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Manganese in PDB 3lp7: Crystal Structure of Human Arginase I in Complex with Inhibitor N(Omega)-Hydroxy-L-Arginine (Noha), 2.04A Resolution

Enzymatic activity of Crystal Structure of Human Arginase I in Complex with Inhibitor N(Omega)-Hydroxy-L-Arginine (Noha), 2.04A Resolution

All present enzymatic activity of Crystal Structure of Human Arginase I in Complex with Inhibitor N(Omega)-Hydroxy-L-Arginine (Noha), 2.04A Resolution:
3.5.3.1;

Protein crystallography data

The structure of Crystal Structure of Human Arginase I in Complex with Inhibitor N(Omega)-Hydroxy-L-Arginine (Noha), 2.04A Resolution, PDB code: 3lp7 was solved by L.Di Costanzo, D.W.Christianson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 34.22 / 2.04
Space group P 3
Cell size a, b, c (Å), α, β, γ (°) 90.680, 90.680, 69.820, 90.00, 90.00, 120.00
R / Rfree (%) 12.3 / 17.4

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of Human Arginase I in Complex with Inhibitor N(Omega)-Hydroxy-L-Arginine (Noha), 2.04A Resolution (pdb code 3lp7). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 4 binding sites of Manganese where determined in the Crystal Structure of Human Arginase I in Complex with Inhibitor N(Omega)-Hydroxy-L-Arginine (Noha), 2.04A Resolution, PDB code: 3lp7:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in 3lp7

Go back to Manganese Binding Sites List in 3lp7
Manganese binding site 1 out of 4 in the Crystal Structure of Human Arginase I in Complex with Inhibitor N(Omega)-Hydroxy-L-Arginine (Noha), 2.04A Resolution


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 Human Arginase I in Complex with Inhibitor N(Omega)-Hydroxy-L-Arginine (Noha), 2.04A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn514

b:15.2
occ:1.00
 OD1 A:ASP124 2.2 11.4 1.0
OH1 A:HAR906 2.2 31.7 1.0
OD1 A:ASP234 2.2 12.3 1.0
OD2 A:ASP232 2.3 14.4 1.0
ND1 A:HIS126 2.3 10.7 1.0
OD2 A:ASP234 2.4 12.6 1.0
CG A:ASP234 2.6 13.3 1.0
NH1 A:HAR906 2.9 34.7 1.0
CE1 A:HIS126 3.0 11.8 1.0
CG A:ASP124 3.1 13.3 1.0
CG A:ASP232 3.3 17.7 1.0
MN A:MN515 3.3 14.5 1.0
OD2 A:ASP124 3.4 12.1 1.0
CG A:HIS126 3.4 13.4 1.0
CZ A:HAR906 3.6 36.9 1.0
NH2 A:HAR906 3.7 38.0 1.0
OD1 A:ASP232 3.9 18.8 1.0
CB A:HIS126 3.9 14.9 1.0
N A:HIS126 4.0 13.0 1.0
N A:ALA125 4.1 13.1 1.0
CB A:ASP234 4.1 13.4 1.0
OG1 A:THR246 4.2 28.5 1.0
NE2 A:HIS126 4.2 11.1 1.0
CB A:ASP232 4.3 16.6 1.0
CD2 A:HIS126 4.4 9.5 1.0
CB A:ASP124 4.5 13.0 1.0
CB A:ALA125 4.6 12.0 1.0
O A:HOH340 4.6 12.8 1.0
CA A:HIS126 4.6 13.6 1.0
NE A:HAR906 4.7 36.6 1.0
CA A:ALA125 4.7 13.0 1.0
C A:ALA125 4.8 11.6 1.0
OD1 A:ASP128 4.8 6.9 1.0
CA A:ASP124 4.9 14.5 1.0
OD2 A:ASP128 4.9 12.6 1.0
C A:ASP124 4.9 13.2 1.0

Manganese binding site 2 out of 4 in 3lp7

Go back to Manganese Binding Sites List in 3lp7
Manganese binding site 2 out of 4 in the Crystal Structure of Human Arginase I in Complex with Inhibitor N(Omega)-Hydroxy-L-Arginine (Noha), 2.04A Resolution


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 Human Arginase I in Complex with Inhibitor N(Omega)-Hydroxy-L-Arginine (Noha), 2.04A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn515

b:14.5
occ:1.00
 OH1 A:HAR906 2.0 31.7 1.0
OD2 A:ASP124 2.1 12.1 1.0
ND1 A:HIS101 2.2 13.2 1.0
OD2 A:ASP128 2.2 12.6 1.0
OD2 A:ASP232 2.5 14.4 1.0
NH1 A:HAR906 3.0 34.7 1.0
CE1 A:HIS101 3.1 15.4 1.0
CG A:ASP124 3.1 13.3 1.0
CG A:HIS101 3.2 12.6 1.0
CG A:ASP128 3.2 11.9 1.0
MN A:MN514 3.3 15.2 1.0
CG A:ASP232 3.4 17.7 1.0
OD1 A:ASP124 3.5 11.4 1.0
CB A:HIS101 3.5 13.8 1.0
OD1 A:ASP128 3.6 6.9 1.0
CB A:ASP232 3.8 16.6 1.0
CZ A:HAR906 4.0 36.9 1.0
NE2 A:HIS101 4.2 15.3 1.0
CD2 A:HIS101 4.3 14.9 1.0
NH2 A:HAR906 4.3 38.0 1.0
CB A:ASP124 4.4 13.0 1.0
O A:HIS141 4.4 19.0 1.0
NE1 A:TRP122 4.4 16.4 1.0
OD1 A:ASP232 4.5 18.8 1.0
CZ2 A:TRP122 4.5 16.3 1.0
CB A:ASP128 4.6 14.9 1.0
OE2 A:GLU277 4.6 18.5 1.0
CG A:GLU277 4.7 18.5 1.0
CE2 A:TRP122 4.8 15.1 1.0
ND1 A:HIS126 4.9 10.7 1.0

Manganese binding site 3 out of 4 in 3lp7

Go back to Manganese Binding Sites List in 3lp7
Manganese binding site 3 out of 4 in the Crystal Structure of Human Arginase I in Complex with Inhibitor N(Omega)-Hydroxy-L-Arginine (Noha), 2.04A Resolution


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 Human Arginase I in Complex with Inhibitor N(Omega)-Hydroxy-L-Arginine (Noha), 2.04A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn514

b:17.4
occ:1.00
 OH1 B:HAR908 2.2 36.1 1.0
OD1 B:ASP234 2.2 21.3 1.0
ND1 B:HIS126 2.3 16.1 1.0
OD2 B:ASP232 2.4 13.9 1.0
OD1 B:ASP124 2.4 16.1 1.0
OD2 B:ASP234 2.5 19.8 1.0
CG B:ASP234 2.7 22.1 1.0
NH1 B:HAR908 3.0 39.3 1.0
CE1 B:HIS126 3.0 17.2 1.0
CG B:ASP232 3.2 17.8 1.0
CG B:ASP124 3.3 16.5 1.0
MN B:MN515 3.4 21.2 1.0
NH2 B:HAR908 3.4 40.4 1.0
CG B:HIS126 3.4 18.5 1.0
OD2 B:ASP124 3.5 15.9 1.0
CZ B:HAR908 3.5 40.6 1.0
OD1 B:ASP232 3.6 17.5 1.0
CB B:HIS126 3.9 18.1 1.0
N B:HIS126 4.0 16.7 1.0
CB B:ASP232 4.1 16.5 1.0
CB B:ASP234 4.2 19.1 1.0
N B:ALA125 4.2 14.9 1.0
NE2 B:HIS126 4.2 18.1 1.0
OG1 B:THR246 4.4 33.7 1.0
CD2 B:HIS126 4.5 17.9 1.0
CA B:HIS126 4.5 18.1 1.0
O B:HOH354 4.6 29.5 1.0
CB B:ALA125 4.6 15.8 1.0
NE B:HAR908 4.7 39.8 1.0
CB B:ASP124 4.7 15.2 1.0
OD1 B:ASP128 4.8 17.4 1.0
C B:ALA125 4.8 14.4 1.0
CA B:ALA125 4.8 15.5 1.0
OD2 B:ASP128 4.8 15.0 1.0
CG B:GLU277 5.0 31.5 1.0

Manganese binding site 4 out of 4 in 3lp7

Go back to Manganese Binding Sites List in 3lp7
Manganese binding site 4 out of 4 in the Crystal Structure of Human Arginase I in Complex with Inhibitor N(Omega)-Hydroxy-L-Arginine (Noha), 2.04A Resolution


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 Human Arginase I in Complex with Inhibitor N(Omega)-Hydroxy-L-Arginine (Noha), 2.04A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn515

b:21.2
occ:1.00
 OH1 B:HAR908 2.1 36.1 1.0
OD2 B:ASP128 2.2 15.0 1.0
OD2 B:ASP124 2.2 15.9 1.0
ND1 B:HIS101 2.2 23.4 1.0
OD2 B:ASP232 2.4 13.9 1.0
NH1 B:HAR908 3.1 39.3 1.0
CE1 B:HIS101 3.1 21.9 1.0
CG B:ASP128 3.2 16.1 1.0
CG B:HIS101 3.2 23.0 1.0
CG B:ASP124 3.2 16.5 1.0
CG B:ASP232 3.4 17.8 1.0
MN B:MN514 3.4 17.4 1.0
CB B:HIS101 3.5 22.9 1.0
OD1 B:ASP128 3.6 17.4 1.0
OD1 B:ASP124 3.6 16.1 1.0
CB B:ASP232 3.6 16.5 1.0
CZ B:HAR908 4.2 40.6 1.0
NE2 B:HIS101 4.3 21.7 1.0
NE1 B:TRP122 4.3 19.2 1.0
CD2 B:HIS101 4.3 24.4 1.0
CB B:ASP128 4.5 16.8 1.0
NH2 B:HAR908 4.5 40.4 1.0
OD1 B:ASP232 4.5 17.5 1.0
CB B:ASP124 4.5 15.2 1.0
CZ2 B:TRP122 4.5 19.0 1.0
O B:HIS141 4.5 27.6 1.0
CG B:GLU277 4.7 31.5 1.0
CE2 B:TRP122 4.7 19.7 1.0
O B:HIS126 4.9 19.8 1.0
ND1 B:HIS126 4.9 16.1 1.0
CA B:ASP232 5.0 18.5 1.0

Reference:

L.Di Costanzo, M.Ilies, K.J.Thorn, D.W.Christianson. Inhibition of Human Arginase I By Substrate and Product Analogues. Arch.Biochem.Biophys. V. 496 101 2010.
ISSN: ISSN 0003-9861
PubMed: 20153713
DOI: 10.1016/J.ABB.2010.02.004
Page generated: Tue Dec 15 04:11:56 2020

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