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Manganese in PDB 1pq3: Human Arginase II: Crystal Structure and Physiological Role in Male and Female Sexual Arousal

Enzymatic activity of Human Arginase II: Crystal Structure and Physiological Role in Male and Female Sexual Arousal

All present enzymatic activity of Human Arginase II: Crystal Structure and Physiological Role in Male and Female Sexual Arousal:
3.5.3.1;

Protein crystallography data

The structure of Human Arginase II: Crystal Structure and Physiological Role in Male and Female Sexual Arousal, PDB code: 1pq3 was solved by E.Cama, D.M.Colleluori, F.A.Emig, H.Shin, S.W.Kim, N.N.Kim, A.M.Traish, D.E.Ash, D.W.Christianson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.70
Space group P 32
Cell size a, b, c (Å), α, β, γ (°) 142.994, 142.994, 127.328, 90.00, 90.00, 120.00
R / Rfree (%) 22.7 / 24.7

Other elements in 1pq3:

The structure of Human Arginase II: Crystal Structure and Physiological Role in Male and Female Sexual Arousal also contains other interesting chemical elements:

Chlorine (Cl) 5 atoms

Manganese Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 12;

Binding sites:

The binding sites of Manganese atom in the Human Arginase II: Crystal Structure and Physiological Role in Male and Female Sexual Arousal (pdb code 1pq3). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 12 binding sites of Manganese where determined in the Human Arginase II: Crystal Structure and Physiological Role in Male and Female Sexual Arousal, PDB code: 1pq3:
Jump to Manganese binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Manganese binding site 1 out of 12 in 1pq3

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Manganese binding site 1 out of 12 in the Human Arginase II: Crystal Structure and Physiological Role in Male and Female Sexual Arousal


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Human Arginase II: Crystal Structure and Physiological Role in Male and Female Sexual Arousal within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn500

b:12.0
occ:1.00
 OD2 A:ASP143 2.0 6.4 1.0
OD2 A:ASP147 2.1 18.6 1.0
OD2 A:ASP251 2.2 9.2 1.0
ND1 A:HIS120 2.4 10.9 1.0
O2 A:S2C551 2.5 18.4 1.0
O1 A:S2C551 2.5 14.8 1.0
B A:S2C551 3.0 17.0 1.0
CG A:ASP147 3.0 20.1 1.0
CG A:ASP143 3.1 11.3 1.0
OD1 A:ASP147 3.3 20.1 1.0
MN A:MN501 3.3 7.3 1.0
CG A:HIS120 3.3 10.9 1.0
CG A:ASP251 3.3 9.8 1.0
O3 A:S2C551 3.4 17.4 1.0
CE1 A:HIS120 3.4 9.8 1.0
CB A:HIS120 3.5 9.3 1.0
OD1 A:ASP143 3.6 11.4 1.0
CB A:ASP251 3.7 9.7 1.0
NE1 A:TRP141 4.3 11.8 1.0
CB A:ASP143 4.3 12.4 1.0
CB A:ASP147 4.4 18.1 1.0
OD1 A:ASP251 4.4 7.8 1.0
CE A:S2C551 4.4 17.9 1.0
CD2 A:HIS120 4.4 9.6 1.0
NE2 A:HIS120 4.5 9.4 1.0
O A:HIS160 4.5 12.4 1.0
CZ2 A:TRP141 4.6 11.8 1.0
CE2 A:TRP141 4.8 12.3 1.0
CG A:GLU296 4.9 16.1 1.0
OD2 A:ASP253 4.9 7.8 1.0
CD A:S2C551 4.9 19.4 1.0
OE2 A:GLU296 5.0 17.4 1.0

Manganese binding site 2 out of 12 in 1pq3

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Manganese binding site 2 out of 12 in the Human Arginase II: Crystal Structure and Physiological Role in Male and Female Sexual Arousal


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Human Arginase II: Crystal Structure and Physiological Role in Male and Female Sexual Arousal within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn501

b:7.3
occ:1.00
 OD1 A:ASP143 2.1 11.4 1.0
OD2 A:ASP253 2.2 7.8 1.0
ND1 A:HIS145 2.3 19.1 1.0
O1 A:S2C551 2.5 14.8 1.0
OD1 A:ASP253 2.5 9.0 1.0
O3 A:S2C551 2.6 17.4 1.0
OD2 A:ASP251 2.6 9.2 1.0
CG A:ASP253 2.7 8.7 1.0
CG A:ASP143 2.9 11.3 1.0
CE1 A:HIS145 3.0 18.2 1.0
B A:S2C551 3.1 17.0 1.0
OD2 A:ASP143 3.1 6.4 1.0
CG A:ASP251 3.2 9.8 1.0
MN A:MN500 3.3 12.0 1.0
CG A:HIS145 3.4 18.7 1.0
OD1 A:ASP251 3.6 7.8 1.0
CB A:HIS145 3.8 17.9 1.0
N A:HIS145 3.9 15.3 1.0
O2 A:S2C551 4.0 18.4 1.0
CB A:ASP251 4.0 9.7 1.0
N A:ALA144 4.0 14.6 1.0
NE2 A:HIS145 4.2 19.0 1.0
CB A:ASP253 4.2 7.6 1.0
CE A:S2C551 4.2 17.9 1.0
CD2 A:HIS145 4.3 18.2 1.0
CB A:ASP143 4.3 12.4 1.0
O A:HOH1205 4.4 41.7 1.0
CA A:HIS145 4.5 17.1 1.0
OD1 A:ASP147 4.6 20.1 1.0
CB A:ALA144 4.7 12.2 1.0
OD2 A:ASP147 4.7 18.6 1.0
CA A:ALA144 4.8 15.0 1.0
C A:ALA144 4.8 14.9 1.0
CA A:ASP143 4.8 14.3 1.0
CD A:S2C551 4.9 19.4 1.0
C A:ASP143 4.9 14.7 1.0

Manganese binding site 3 out of 12 in 1pq3

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Manganese binding site 3 out of 12 in the Human Arginase II: Crystal Structure and Physiological Role in Male and Female Sexual Arousal


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Human Arginase II: Crystal Structure and Physiological Role in Male and Female Sexual Arousal within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn502

b:15.0
occ:1.00
 OD2 B:ASP143 2.0 1.3 1.0
OD2 B:ASP251 2.2 16.8 1.0
OD2 B:ASP147 2.2 19.5 1.0
ND1 B:HIS120 2.3 6.1 1.0
O2 B:S2C552 2.5 19.9 1.0
O1 B:S2C552 2.5 19.2 1.0
B B:S2C552 2.9 19.7 1.0
CG B:ASP143 3.1 4.4 1.0
CG B:HIS120 3.2 8.2 1.0
CG B:ASP251 3.2 15.8 1.0
CG B:ASP147 3.2 16.6 1.0
CE1 B:HIS120 3.3 7.3 1.0
MN B:MN503 3.3 11.2 1.0
O3 B:S2C552 3.3 19.1 1.0
CB B:HIS120 3.4 9.9 1.0
OD1 B:ASP143 3.5 7.0 1.0
OD1 B:ASP147 3.5 15.9 1.0
CB B:ASP251 3.6 15.1 1.0
OD1 B:ASP251 4.3 17.8 1.0
CD2 B:HIS120 4.4 6.9 1.0
NE2 B:HIS120 4.4 6.3 1.0
CB B:ASP143 4.4 6.1 1.0
CE B:S2C552 4.4 21.9 1.0
NE1 B:TRP141 4.4 11.5 1.0
CB B:ASP147 4.6 14.2 1.0
O B:HIS160 4.6 17.8 1.0
CG B:GLU296 4.7 18.9 1.0
CZ2 B:TRP141 4.8 8.3 1.0
OD2 B:ASP253 4.8 8.1 1.0
OD1 B:ASP253 4.8 11.2 1.0
OE2 B:GLU296 4.9 17.9 1.0
CA B:HIS120 4.9 10.7 1.0
CD B:S2C552 5.0 22.6 1.0
CE2 B:TRP141 5.0 10.6 1.0
CA B:ASP251 5.0 12.9 1.0

Manganese binding site 4 out of 12 in 1pq3

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Manganese binding site 4 out of 12 in the Human Arginase II: Crystal Structure and Physiological Role in Male and Female Sexual Arousal


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Human Arginase II: Crystal Structure and Physiological Role in Male and Female Sexual Arousal within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn503

b:11.2
occ:1.00
 OD1 B:ASP143 2.1 7.0 1.0
ND1 B:HIS145 2.4 10.9 1.0
OD2 B:ASP253 2.4 8.1 1.0
OD1 B:ASP253 2.5 11.2 1.0
O1 B:S2C552 2.5 19.2 1.0
OD2 B:ASP251 2.6 16.8 1.0
O3 B:S2C552 2.7 19.1 1.0
CG B:ASP253 2.8 11.8 1.0
CG B:ASP143 3.0 4.4 1.0
B B:S2C552 3.2 19.7 1.0
CE1 B:HIS145 3.2 10.3 1.0
OD2 B:ASP143 3.3 1.3 1.0
CG B:ASP251 3.3 15.8 1.0
MN B:MN502 3.3 15.0 1.0
CG B:HIS145 3.4 11.1 1.0
CB B:HIS145 3.7 10.4 1.0
OD1 B:ASP251 3.8 17.8 1.0
N B:HIS145 3.8 11.1 1.0
N B:ALA144 4.0 8.0 1.0
O2 B:S2C552 4.1 19.9 1.0
CB B:ASP251 4.2 15.1 1.0
CB B:ASP253 4.2 10.8 1.0
CE B:S2C552 4.3 21.9 1.0
CB B:ASP143 4.4 6.1 1.0
NE2 B:HIS145 4.4 9.3 1.0
CA B:HIS145 4.4 11.3 1.0
OG1 B:THR265 4.4 25.2 1.0
CD2 B:HIS145 4.5 10.3 1.0
CB B:ALA144 4.5 8.4 1.0
OD1 B:ASP147 4.6 15.9 1.0
C B:ALA144 4.6 11.1 1.0
CA B:ALA144 4.6 9.4 1.0
OD2 B:ASP147 4.7 19.5 1.0
CA B:ASP143 4.8 7.2 1.0
C B:ASP143 4.8 7.9 1.0
CD B:S2C552 4.9 22.6 1.0

Manganese binding site 5 out of 12 in 1pq3

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Manganese binding site 5 out of 12 in the Human Arginase II: Crystal Structure and Physiological Role in Male and Female Sexual Arousal


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 5 of Human Arginase II: Crystal Structure and Physiological Role in Male and Female Sexual Arousal within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mn504

b:10.1
occ:1.00
 OD1 C:ASP143 2.1 16.2 1.0
OD2 C:ASP253 2.2 8.4 1.0
ND1 C:HIS145 2.3 13.5 1.0
OD1 C:ASP253 2.5 12.5 1.0
O1 C:S2C553 2.5 24.3 1.0
OD2 C:ASP251 2.5 7.8 1.0
CG C:ASP253 2.7 11.4 1.0
O3 C:S2C553 2.7 24.1 1.0
CE1 C:HIS145 2.9 13.8 1.0
CG C:ASP143 3.0 16.4 1.0
CG C:ASP251 3.2 12.9 1.0
B C:S2C553 3.2 24.9 1.0
MN C:MN505 3.3 15.8 1.0
OD2 C:ASP143 3.3 20.4 1.0
CG C:HIS145 3.5 13.9 1.0
OD1 C:ASP251 3.6 13.2 1.0
N C:HIS145 3.9 17.7 1.0
N C:ALA144 4.0 14.8 1.0
CB C:HIS145 4.0 16.5 1.0
CB C:ASP251 4.1 13.9 1.0
O2 C:S2C553 4.1 25.3 1.0
NE2 C:HIS145 4.1 15.2 1.0
CB C:ASP253 4.2 11.6 1.0
CE C:S2C553 4.3 26.4 1.0
OG1 C:THR265 4.3 25.6 1.0
CB C:ASP143 4.4 16.5 1.0
CD2 C:HIS145 4.4 13.9 1.0
CB C:ALA144 4.5 15.9 1.0
CA C:HIS145 4.6 16.8 1.0
OD1 C:ASP147 4.7 18.6 1.0
CA C:ALA144 4.7 16.3 1.0
OD2 C:ASP147 4.7 17.7 1.0
C C:ALA144 4.7 17.4 1.0
O C:HOH970 4.8 12.1 1.0
CA C:ASP143 4.8 15.9 1.0
CD C:S2C553 4.9 27.7 1.0
C C:ASP143 4.9 15.1 1.0

Manganese binding site 6 out of 12 in 1pq3

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Manganese binding site 6 out of 12 in the Human Arginase II: Crystal Structure and Physiological Role in Male and Female Sexual Arousal


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 6 of Human Arginase II: Crystal Structure and Physiological Role in Male and Female Sexual Arousal within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mn505

b:15.8
occ:1.00
 OD2 C:ASP143 2.0 20.4 1.0
OD2 C:ASP147 2.1 17.7 1.0
OD2 C:ASP251 2.2 7.8 1.0
ND1 C:HIS120 2.4 16.4 1.0
O1 C:S2C553 2.4 24.3 1.0
O2 C:S2C553 2.5 25.3 1.0
B C:S2C553 2.9 24.9 1.0
CG C:ASP143 3.0 16.4 1.0
CG C:ASP147 3.1 18.1 1.0
CG C:ASP251 3.2 12.9 1.0
MN C:MN504 3.3 10.1 1.0
OD1 C:ASP147 3.3 18.6 1.0
CG C:HIS120 3.3 17.1 1.0
O3 C:S2C553 3.3 24.1 1.0
CE1 C:HIS120 3.3 17.3 1.0
OD1 C:ASP143 3.4 16.2 1.0
CB C:HIS120 3.5 16.8 1.0
CB C:ASP251 3.7 13.9 1.0
NE1 C:TRP141 4.3 16.4 1.0
CB C:ASP143 4.3 16.5 1.0
OD1 C:ASP251 4.4 13.2 1.0
CE C:S2C553 4.4 26.4 1.0
NE2 C:HIS120 4.4 15.4 1.0
CD2 C:HIS120 4.5 16.6 1.0
CB C:ASP147 4.5 16.8 1.0
O C:HIS160 4.5 19.1 1.0
CZ2 C:TRP141 4.7 16.4 1.0
CG C:GLU296 4.8 17.9 1.0
CE2 C:TRP141 4.9 17.3 1.0
OD2 C:ASP253 4.9 8.4 1.0
OE2 C:GLU296 4.9 18.2 1.0
CD C:S2C553 4.9 27.7 1.0
ND1 C:HIS145 5.0 13.5 1.0
CA C:ASP251 5.0 13.7 1.0

Manganese binding site 7 out of 12 in 1pq3

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Manganese binding site 7 out of 12 in the Human Arginase II: Crystal Structure and Physiological Role in Male and Female Sexual Arousal


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 7 of Human Arginase II: Crystal Structure and Physiological Role in Male and Female Sexual Arousal within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mn506

b:11.2
occ:1.00
 OD2 D:ASP143 2.0 6.5 1.0
OD2 D:ASP147 2.1 18.5 1.0
OD2 D:ASP251 2.2 9.1 1.0
ND1 D:HIS120 2.4 11.0 1.0
O2 D:S2C554 2.5 16.8 1.0
O1 D:S2C554 2.5 12.6 1.0
B D:S2C554 3.0 15.8 1.0
CG D:ASP147 3.0 20.0 1.0
CG D:ASP143 3.1 11.3 1.0
OD1 D:ASP147 3.3 20.0 1.0
MN D:MN507 3.3 8.0 1.0
CG D:HIS120 3.3 10.9 1.0
CG D:ASP251 3.3 9.8 1.0
CE1 D:HIS120 3.4 9.8 1.0
O3 D:S2C554 3.4 15.5 1.0
CB D:HIS120 3.5 9.3 1.0
OD1 D:ASP143 3.6 11.4 1.0
CB D:ASP251 3.7 9.8 1.0
NE1 D:TRP141 4.3 11.8 1.0
CB D:ASP143 4.3 12.4 1.0
CB D:ASP147 4.4 18.1 1.0
OD1 D:ASP251 4.4 7.8 1.0
CE D:S2C554 4.4 16.7 1.0
CD2 D:HIS120 4.4 9.5 1.0
NE2 D:HIS120 4.5 9.4 1.0
O D:HIS160 4.5 12.4 1.0
CZ2 D:TRP141 4.6 11.7 1.0
CE2 D:TRP141 4.8 12.3 1.0
CG D:GLU296 4.9 16.1 1.0
OD2 D:ASP253 4.9 7.8 1.0
OE2 D:GLU296 4.9 17.4 1.0
CD D:S2C554 4.9 18.7 1.0

Manganese binding site 8 out of 12 in 1pq3

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Manganese binding site 8 out of 12 in the Human Arginase II: Crystal Structure and Physiological Role in Male and Female Sexual Arousal


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 8 of Human Arginase II: Crystal Structure and Physiological Role in Male and Female Sexual Arousal within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mn507

b:8.0
occ:1.00
 OD1 D:ASP143 2.1 11.4 1.0
OD2 D:ASP253 2.3 7.8 1.0
ND1 D:HIS145 2.3 19.1 1.0
OD1 D:ASP253 2.5 9.0 1.0
O1 D:S2C554 2.5 12.6 1.0
OD2 D:ASP251 2.6 9.1 1.0
O3 D:S2C554 2.6 15.5 1.0
CG D:ASP253 2.7 8.7 1.0
CG D:ASP143 3.0 11.3 1.0
CE1 D:HIS145 3.0 18.3 1.0
B D:S2C554 3.1 15.8 1.0
OD2 D:ASP143 3.1 6.5 1.0
CG D:ASP251 3.2 9.8 1.0
MN D:MN506 3.3 11.2 1.0
CG D:HIS145 3.4 18.5 1.0
OD1 D:ASP251 3.6 7.8 1.0
CB D:HIS145 3.8 17.9 1.0
N D:HIS145 3.9 15.4 1.0
O2 D:S2C554 4.0 16.8 1.0
CB D:ASP251 4.0 9.8 1.0
N D:ALA144 4.1 14.6 1.0
NE2 D:HIS145 4.1 18.9 1.0
CB D:ASP253 4.2 7.7 1.0
CE D:S2C554 4.2 16.7 1.0
CD2 D:HIS145 4.3 18.3 1.0
CB D:ASP143 4.3 12.4 1.0
CA D:HIS145 4.5 17.1 1.0
OD1 D:ASP147 4.7 20.0 1.0
CB D:ALA144 4.7 12.2 1.0
OD2 D:ASP147 4.7 18.5 1.0
CA D:ALA144 4.8 15.0 1.0
C D:ALA144 4.8 14.9 1.0
CA D:ASP143 4.8 14.3 1.0
CD D:S2C554 4.9 18.7 1.0
C D:ASP143 4.9 14.8 1.0

Manganese binding site 9 out of 12 in 1pq3

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Manganese binding site 9 out of 12 in the Human Arginase II: Crystal Structure and Physiological Role in Male and Female Sexual Arousal


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 9 of Human Arginase II: Crystal Structure and Physiological Role in Male and Female Sexual Arousal within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Mn508

b:14.6
occ:1.00
 OD2 E:ASP143 2.0 1.4 1.0
OD2 E:ASP251 2.2 16.9 1.0
OD2 E:ASP147 2.2 19.5 1.0
ND1 E:HIS120 2.3 6.2 1.0
O2 E:S2C555 2.5 21.7 1.0
O1 E:S2C555 2.6 20.9 1.0
B E:S2C555 2.9 20.9 1.0
CG E:ASP143 3.1 4.5 1.0
CG E:HIS120 3.2 8.3 1.0
CG E:ASP147 3.2 16.6 1.0
CG E:ASP251 3.2 15.7 1.0
O3 E:S2C555 3.3 18.6 1.0
CE1 E:HIS120 3.3 7.3 1.0
MN E:MN509 3.3 11.4 1.0
CB E:HIS120 3.4 9.8 1.0
OD1 E:ASP143 3.5 6.9 1.0
OD1 E:ASP147 3.5 15.9 1.0
CB E:ASP251 3.6 15.0 1.0
OD1 E:ASP251 4.3 17.7 1.0
CD2 E:HIS120 4.4 6.8 1.0
NE2 E:HIS120 4.4 6.3 1.0
CB E:ASP143 4.4 6.1 1.0
CE E:S2C555 4.4 22.8 1.0
NE1 E:TRP141 4.4 11.4 1.0
CB E:ASP147 4.6 14.2 1.0
O E:HIS160 4.6 17.6 1.0
CG E:GLU296 4.7 18.9 1.0
CZ2 E:TRP141 4.8 8.3 1.0
OD2 E:ASP253 4.8 8.0 1.0
OD1 E:ASP253 4.8 11.2 1.0
OE2 E:GLU296 4.9 17.8 1.0
CA E:HIS120 4.9 10.7 1.0
CE2 E:TRP141 5.0 10.6 1.0
CD E:S2C555 5.0 22.9 1.0
CA E:ASP251 5.0 13.0 1.0

Manganese binding site 10 out of 12 in 1pq3

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Manganese binding site 10 out of 12 in the Human Arginase II: Crystal Structure and Physiological Role in Male and Female Sexual Arousal


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 10 of Human Arginase II: Crystal Structure and Physiological Role in Male and Female Sexual Arousal within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Mn509

b:11.4
occ:1.00
 OD1 E:ASP143 2.1 6.9 1.0
ND1 E:HIS145 2.4 10.8 1.0
OD2 E:ASP253 2.5 8.0 1.0
OD1 E:ASP253 2.5 11.2 1.0
O1 E:S2C555 2.5 20.9 1.0
OD2 E:ASP251 2.6 16.9 1.0
O3 E:S2C555 2.7 18.6 1.0
CG E:ASP253 2.8 11.7 1.0
CG E:ASP143 3.0 4.5 1.0
B E:S2C555 3.2 20.9 1.0
CE1 E:HIS145 3.2 10.3 1.0
OD2 E:ASP143 3.2 1.4 1.0
CG E:ASP251 3.3 15.7 1.0
MN E:MN508 3.3 14.6 1.0
CG E:HIS145 3.4 11.0 1.0
CB E:HIS145 3.7 10.4 1.0
OD1 E:ASP251 3.8 17.7 1.0
N E:HIS145 3.8 10.9 1.0
N E:ALA144 4.0 8.0 1.0
O2 E:S2C555 4.1 21.7 1.0
CB E:ASP251 4.1 15.0 1.0
CB E:ASP253 4.2 10.7 1.0
CE E:S2C555 4.3 22.8 1.0
CB E:ASP143 4.4 6.1 1.0
NE2 E:HIS145 4.4 9.4 1.0
CA E:HIS145 4.4 11.2 1.0
OG1 E:THR265 4.4 25.2 1.0
CD2 E:HIS145 4.5 10.3 1.0
CB E:ALA144 4.5 8.3 1.0
OD1 E:ASP147 4.6 15.9 1.0
C E:ALA144 4.6 11.1 1.0
CA E:ALA144 4.6 9.3 1.0
OD2 E:ASP147 4.7 19.5 1.0
CA E:ASP143 4.8 7.2 1.0
C E:ASP143 4.8 8.0 1.0
CD E:S2C555 4.9 22.9 1.0
O E:HOH1003 4.9 13.4 1.0
O E:HIS145 5.0 12.7 1.0

Reference:

E.Cama, D.M.Colleluori, F.A.Emig, H.Shin, S.W.Kim, N.N.Kim, A.M.Traish, D.E.Ash, D.W.Christianson. Human Arginase II: Crystal Structure and Physiological Role in Male and Female Sexual Arousal Biochemistry V. 42 8445 2003.
ISSN: ISSN 0006-2960
PubMed: 12859189
DOI: 10.1021/BI034340J
Page generated: Tue Dec 15 03:54:28 2020

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