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Manganese in PDB 1hqf: Crystal Structure of the Binuclear Manganese Metalloenzyme Arginase Complexed with N-Hydroxy-L-Arginine

Enzymatic activity of Crystal Structure of the Binuclear Manganese Metalloenzyme Arginase Complexed with N-Hydroxy-L-Arginine

All present enzymatic activity of Crystal Structure of the Binuclear Manganese Metalloenzyme Arginase Complexed with N-Hydroxy-L-Arginine:
3.5.3.1;

Protein crystallography data

The structure of Crystal Structure of the Binuclear Manganese Metalloenzyme Arginase Complexed with N-Hydroxy-L-Arginine, PDB code: 1hqf was solved by J.D.Cox, E.Cama, D.M.Colleluori, 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 / 2.90
Space group P 32
Cell size a, b, c (Å), α, β, γ (°) 88.000, 88.000, 112.000, 90.00, 90.00, 120.00
R / Rfree (%) 26.5 / 28.9

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of the Binuclear Manganese Metalloenzyme Arginase Complexed with N-Hydroxy-L-Arginine (pdb code 1hqf). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 6 binding sites of Manganese where determined in the Crystal Structure of the Binuclear Manganese Metalloenzyme Arginase Complexed with N-Hydroxy-L-Arginine, PDB code: 1hqf:
Jump to Manganese binding site number: 1; 2; 3; 4; 5; 6;

Manganese binding site 1 out of 6 in 1hqf

Go back to Manganese Binding Sites List in 1hqf
Manganese binding site 1 out of 6 in the Crystal Structure of the Binuclear Manganese Metalloenzyme Arginase Complexed with N-Hydroxy-L-Arginine


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of the Binuclear Manganese Metalloenzyme Arginase Complexed with N-Hydroxy-L-Arginine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn500

b:67.5
occ:1.00
 OD2 A:ASP124 2.0 46.8 1.0
OD2 A:ASP128 2.1 71.2 1.0
ND1 A:HIS101 2.4 85.5 1.0
OH1 A:HAR906 2.6 52.9 1.0
CG A:HIS101 3.0 86.6 1.0
NH1 A:HAR906 3.0 53.1 1.0
CG A:ASP128 3.1 74.4 1.0
CB A:HIS101 3.1 86.7 1.0
OD2 A:ASP232 3.1 54.4 1.0
CG A:ASP124 3.1 47.6 1.0
CE1 A:HIS101 3.4 86.4 1.0
CZ A:HAR906 3.5 53.0 1.0
OD1 A:ASP128 3.6 74.7 1.0
OD1 A:ASP124 3.6 46.9 1.0
NH2 A:HAR906 3.7 53.7 1.0
MN A:MN501 3.9 57.0 1.0
CG A:ASP232 4.0 54.2 1.0
O A:HIS141 4.0 93.6 1.0
CD2 A:HIS101 4.1 86.3 1.0
CZ2 A:TRP122 4.1 54.6 1.0
CB A:ASP128 4.2 76.1 1.0
OE2 A:GLU277 4.2 63.0 1.0
NE2 A:HIS101 4.2 86.7 1.0
CB A:ASP124 4.4 50.7 1.0
CB A:ASP232 4.4 53.8 1.0
NE A:HAR906 4.5 55.1 1.0
CG A:GLU277 4.5 60.0 1.0
NE1 A:TRP122 4.5 55.2 1.0
CA A:HIS101 4.6 85.7 1.0
CE2 A:TRP122 4.6 55.0 1.0
OD2 A:ASP234 4.7 66.8 1.0
CD A:GLU277 4.8 60.4 1.0
OD1 A:ASP232 4.8 51.2 1.0
ND1 A:HIS126 4.9 59.2 1.0

Manganese binding site 2 out of 6 in 1hqf

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Manganese binding site 2 out of 6 in the Crystal Structure of the Binuclear Manganese Metalloenzyme Arginase Complexed with N-Hydroxy-L-Arginine


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of the Binuclear Manganese Metalloenzyme Arginase Complexed with N-Hydroxy-L-Arginine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn501

b:57.0
occ:1.00
 ND1 A:HIS126 2.0 59.2 1.0
OD2 A:ASP234 2.0 66.8 1.0
OD1 A:ASP124 2.2 46.9 1.0
OH1 A:HAR906 2.2 52.9 1.0
NH1 A:HAR906 2.3 53.1 1.0
OD1 A:ASP234 2.5 65.0 1.0
CE1 A:HIS126 2.5 59.0 1.0
OD2 A:ASP232 2.5 54.4 1.0
CG A:ASP234 2.5 64.0 1.0
CG A:ASP124 3.1 47.6 1.0
CG A:HIS126 3.3 57.0 1.0
OD2 A:ASP124 3.3 46.8 1.0
O A:HOH601 3.4 30.8 1.0
CG A:ASP232 3.6 54.2 1.0
CZ A:HAR906 3.7 53.0 1.0
NE2 A:HIS126 3.8 58.7 1.0
N A:ALA125 3.8 56.4 1.0
N A:HIS126 3.8 59.9 1.0
MN A:MN500 3.9 67.5 1.0
CB A:HIS126 4.0 58.5 1.0
CB A:ASP234 4.0 59.0 1.0
CD2 A:HIS126 4.1 55.9 1.0
OD1 A:ASP232 4.1 51.2 1.0
CB A:ALA125 4.2 56.1 1.0
CB A:ASP124 4.4 50.7 1.0
CD A:HAR906 4.4 57.5 1.0
NE A:HAR906 4.4 55.1 1.0
CA A:ALA125 4.5 57.6 1.0
NH2 A:HAR906 4.5 53.7 1.0
CA A:HIS126 4.5 61.1 1.0
OD2 A:ASP128 4.5 71.2 1.0
OD1 A:ASP128 4.6 74.7 1.0
CA A:ASP124 4.6 54.2 1.0
C A:ASP124 4.6 55.3 1.0
C A:ALA125 4.6 58.3 1.0
CB A:ASP232 4.7 53.8 1.0
CG A:GLU277 4.9 60.0 1.0

Manganese binding site 3 out of 6 in 1hqf

Go back to Manganese Binding Sites List in 1hqf
Manganese binding site 3 out of 6 in the Crystal Structure of the Binuclear Manganese Metalloenzyme Arginase Complexed with N-Hydroxy-L-Arginine


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Crystal Structure of the Binuclear Manganese Metalloenzyme Arginase Complexed with N-Hydroxy-L-Arginine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn502

b:67.5
occ:1.00
 OD2 B:ASP124 2.0 46.8 1.0
OD2 B:ASP128 2.1 71.2 1.0
ND1 B:HIS101 2.4 85.5 1.0
OH1 B:HAR907 2.6 52.9 1.0
CG B:HIS101 3.0 86.6 1.0
NH1 B:HAR907 3.0 53.1 1.0
CG B:ASP128 3.1 74.4 1.0
CB B:HIS101 3.1 86.7 1.0
OD2 B:ASP232 3.1 54.4 1.0
CG B:ASP124 3.1 47.6 1.0
CE1 B:HIS101 3.4 86.4 1.0
CZ B:HAR907 3.5 53.0 1.0
OD1 B:ASP128 3.6 74.7 1.0
OD1 B:ASP124 3.6 46.9 1.0
NH2 B:HAR907 3.7 53.7 1.0
MN B:MN503 3.9 57.0 1.0
CG B:ASP232 4.0 54.2 1.0
O B:HIS141 4.0 93.6 1.0
CD2 B:HIS101 4.1 86.3 1.0
CZ2 B:TRP122 4.1 54.6 1.0
CB B:ASP128 4.2 76.1 1.0
OE2 B:GLU277 4.2 63.0 1.0
NE2 B:HIS101 4.2 86.7 1.0
CB B:ASP124 4.4 50.7 1.0
CB B:ASP232 4.4 53.8 1.0
NE B:HAR907 4.5 55.1 1.0
CG B:GLU277 4.5 60.0 1.0
NE1 B:TRP122 4.5 55.2 1.0
OD2 B:ASP234 4.6 66.8 1.0
CA B:HIS101 4.6 85.7 1.0
CE2 B:TRP122 4.6 55.0 1.0
CD B:GLU277 4.8 60.4 1.0
OD1 B:ASP232 4.8 51.2 1.0
ND1 B:HIS126 4.9 59.2 1.0

Manganese binding site 4 out of 6 in 1hqf

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Manganese binding site 4 out of 6 in the Crystal Structure of the Binuclear Manganese Metalloenzyme Arginase Complexed with N-Hydroxy-L-Arginine


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Crystal Structure of the Binuclear Manganese Metalloenzyme Arginase Complexed with N-Hydroxy-L-Arginine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn503

b:57.0
occ:1.00
 OD2 B:ASP234 1.9 66.8 1.0
ND1 B:HIS126 2.0 59.2 1.0
OD1 B:ASP124 2.2 46.9 1.0
OH1 B:HAR907 2.2 52.9 1.0
NH1 B:HAR907 2.3 53.1 1.0
CE1 B:HIS126 2.5 59.0 1.0
OD2 B:ASP232 2.5 54.4 1.0
CG B:ASP234 2.5 64.0 1.0
OD1 B:ASP234 2.6 65.0 1.0
CG B:ASP124 3.1 47.6 1.0
CG B:HIS126 3.3 57.0 1.0
OD2 B:ASP124 3.3 46.8 1.0
O B:HOH606 3.4 30.8 1.0
CG B:ASP232 3.6 54.2 1.0
CZ B:HAR907 3.7 53.0 1.0
NE2 B:HIS126 3.8 58.7 1.0
N B:ALA125 3.8 56.4 1.0
N B:HIS126 3.8 59.9 1.0
MN B:MN502 3.9 67.5 1.0
CB B:ASP234 3.9 59.0 1.0
CB B:HIS126 4.0 58.5 1.0
CD2 B:HIS126 4.1 55.9 1.0
OD1 B:ASP232 4.1 51.2 1.0
CB B:ALA125 4.2 56.1 1.0
CB B:ASP124 4.4 50.7 1.0
CD B:HAR907 4.4 57.5 1.0
NE B:HAR907 4.4 55.1 1.0
CA B:ALA125 4.5 57.6 1.0
NH2 B:HAR907 4.5 53.7 1.0
CA B:HIS126 4.5 61.1 1.0
OD2 B:ASP128 4.5 71.2 1.0
OD1 B:ASP128 4.6 74.7 1.0
CA B:ASP124 4.6 54.2 1.0
C B:ASP124 4.6 55.3 1.0
C B:ALA125 4.6 58.3 1.0
CB B:ASP232 4.7 53.8 1.0
CG B:GLU277 4.9 60.0 1.0

Manganese binding site 5 out of 6 in 1hqf

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Manganese binding site 5 out of 6 in the Crystal Structure of the Binuclear Manganese Metalloenzyme Arginase Complexed with N-Hydroxy-L-Arginine


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 5 of Crystal Structure of the Binuclear Manganese Metalloenzyme Arginase Complexed with N-Hydroxy-L-Arginine within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mn504

b:67.5
occ:1.00
 OD2 C:ASP124 2.0 46.8 1.0
OD2 C:ASP128 2.1 71.2 1.0
ND1 C:HIS101 2.4 85.5 1.0
OH1 C:HAR908 2.6 52.9 1.0
CG C:HIS101 3.0 86.6 1.0
NH1 C:HAR908 3.0 53.1 1.0
CG C:ASP128 3.1 74.4 1.0
CB C:HIS101 3.1 86.7 1.0
OD2 C:ASP232 3.1 54.4 1.0
CG C:ASP124 3.1 47.6 1.0
CE1 C:HIS101 3.4 86.4 1.0
CZ C:HAR908 3.6 53.0 1.0
OD1 C:ASP128 3.6 74.7 1.0
OD1 C:ASP124 3.6 46.9 1.0
NH2 C:HAR908 3.7 53.7 1.0
MN C:MN505 3.9 57.0 1.0
CG C:ASP232 4.0 54.2 1.0
O C:HIS141 4.0 93.6 1.0
CD2 C:HIS101 4.1 86.3 1.0
CZ2 C:TRP122 4.1 54.6 1.0
CB C:ASP128 4.2 76.1 1.0
OE2 C:GLU277 4.2 63.0 1.0
NE2 C:HIS101 4.2 86.7 1.0
CB C:ASP124 4.4 50.7 1.0
CB C:ASP232 4.4 53.8 1.0
NE C:HAR908 4.5 55.1 1.0
CG C:GLU277 4.5 60.0 1.0
NE1 C:TRP122 4.5 55.2 1.0
OD2 C:ASP234 4.6 66.8 1.0
CA C:HIS101 4.6 85.7 1.0
CE2 C:TRP122 4.6 55.0 1.0
CD C:GLU277 4.8 60.4 1.0
OD1 C:ASP232 4.8 51.2 1.0
ND1 C:HIS126 4.9 59.2 1.0

Manganese binding site 6 out of 6 in 1hqf

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Manganese binding site 6 out of 6 in the Crystal Structure of the Binuclear Manganese Metalloenzyme Arginase Complexed with N-Hydroxy-L-Arginine


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 6 of Crystal Structure of the Binuclear Manganese Metalloenzyme Arginase Complexed with N-Hydroxy-L-Arginine within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mn505

b:57.0
occ:1.00
 OD2 C:ASP234 1.9 66.8 1.0
ND1 C:HIS126 2.0 59.2 1.0
OD1 C:ASP124 2.2 46.9 1.0
OH1 C:HAR908 2.2 52.9 1.0
NH1 C:HAR908 2.3 53.1 1.0
CE1 C:HIS126 2.5 59.0 1.0
OD2 C:ASP232 2.5 54.4 1.0
CG C:ASP234 2.5 64.0 1.0
OD1 C:ASP234 2.6 65.0 1.0
CG C:ASP124 3.1 47.6 1.0
CG C:HIS126 3.3 57.0 1.0
OD2 C:ASP124 3.3 46.8 1.0
O C:HOH611 3.4 30.8 1.0
CG C:ASP232 3.6 54.2 1.0
CZ C:HAR908 3.7 53.0 1.0
NE2 C:HIS126 3.8 58.7 1.0
N C:ALA125 3.8 56.4 1.0
N C:HIS126 3.8 59.9 1.0
MN C:MN504 3.9 67.5 1.0
CB C:ASP234 3.9 59.0 1.0
CB C:HIS126 4.0 58.5 1.0
CD2 C:HIS126 4.1 55.9 1.0
OD1 C:ASP232 4.1 51.2 1.0
CB C:ALA125 4.2 56.1 1.0
CB C:ASP124 4.4 50.7 1.0
CD C:HAR908 4.4 57.5 1.0
NE C:HAR908 4.4 55.1 1.0
CA C:ALA125 4.5 57.6 1.0
NH2 C:HAR908 4.5 53.7 1.0
CA C:HIS126 4.5 61.1 1.0
OD2 C:ASP128 4.5 71.2 1.0
OD1 C:ASP128 4.6 74.7 1.0
CA C:ASP124 4.6 54.2 1.0
C C:ASP124 4.6 55.3 1.0
C C:ALA125 4.6 58.3 1.0
CB C:ASP232 4.7 53.8 1.0
CG C:GLU277 4.9 60.0 1.0

Reference:

J.D.Cox, E.Cama, D.M.Colleluori, S.Pethe, J.L.Boucher, D.Mansuy, D.E.Ash, D.W.Christianson. Mechanistic and Metabolic Inferences From the Binding of Substrate Analogues and Products to Arginase. Biochemistry V. 40 2689 2001.
ISSN: ISSN 0006-2960
PubMed: 11258880
DOI: 10.1021/BI002318+
Page generated: Sat Oct 5 10:54:01 2024

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