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Manganese in PDB 3lp4: Crystal Structure of Human Arginase I in Complex with L-Lysine, 1.90A Resolution.

Enzymatic activity of Crystal Structure of Human Arginase I in Complex with L-Lysine, 1.90A Resolution.

All present enzymatic activity of Crystal Structure of Human Arginase I in Complex with L-Lysine, 1.90A Resolution.:
3.5.3.1;

Protein crystallography data

The structure of Crystal Structure of Human Arginase I in Complex with L-Lysine, 1.90A Resolution., PDB code: 3lp4 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) 34.20 / 1.90
Space group P 3
Cell size a, b, c (Å), α, β, γ (°) 90.729, 90.729, 69.509, 90.00, 90.00, 120.00
R / Rfree (%) 15.5 / 20.4

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of Human Arginase I in Complex with L-Lysine, 1.90A Resolution. (pdb code 3lp4). 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 L-Lysine, 1.90A Resolution., PDB code: 3lp4:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in 3lp4

Go back to Manganese Binding Sites List in 3lp4
Manganese binding site 1 out of 4 in the Crystal Structure of Human Arginase I in Complex with L-Lysine, 1.90A 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 L-Lysine, 1.90A Resolution. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn514

b:18.5
occ:1.00
OD1 A:ASP124 1.9 18.0 1.0
ND1 A:HIS126 2.0 14.4 1.0
OD1 A:ASP234 2.2 17.6 1.0
OD2 A:ASP234 2.5 15.7 1.0
OD2 A:ASP232 2.5 17.0 1.0
CE1 A:HIS126 2.6 13.5 1.0
O A:HOH999 2.7 25.6 1.0
CG A:ASP234 2.7 16.5 1.0
CG A:ASP124 2.9 16.8 1.0
CG A:HIS126 3.2 13.9 1.0
OD2 A:ASP124 3.3 14.8 1.0
MN A:MN515 3.3 14.3 1.0
CG A:ASP232 3.4 18.5 1.0
NZ A:LYS401 3.8 24.7 1.0
NE2 A:HIS126 3.8 15.3 1.0
N A:HIS126 3.9 12.7 1.0
N A:ALA125 3.9 14.3 1.0
CB A:HIS126 3.9 14.9 1.0
OD1 A:ASP232 4.0 14.9 1.0
OG1 A:THR246 4.1 16.5 1.0
CD2 A:HIS126 4.2 13.6 1.0
CB A:ASP234 4.2 15.1 1.0
CB A:ASP124 4.3 16.9 1.0
CB A:ASP232 4.3 17.5 1.0
CE A:LYS401 4.4 23.8 1.0
CB A:ALA125 4.4 9.6 1.0
CA A:HIS126 4.5 13.7 1.0
CA A:ALA125 4.6 12.7 1.0
OD1 A:ASP128 4.6 7.8 1.0
C A:ALA125 4.6 11.3 1.0
O A:HOH345 4.7 14.7 1.0
OD2 A:ASP128 4.7 12.8 1.0
CA A:ASP124 4.7 14.6 1.0
C A:ASP124 4.8 12.8 1.0
CD A:LYS401 4.8 24.2 1.0
O A:THR246 4.8 17.3 1.0

Manganese binding site 2 out of 4 in 3lp4

Go back to Manganese Binding Sites List in 3lp4
Manganese binding site 2 out of 4 in the Crystal Structure of Human Arginase I in Complex with L-Lysine, 1.90A 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 L-Lysine, 1.90A Resolution. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn515

b:14.3
occ:1.00
OD2 A:ASP124 1.9 14.8 1.0
O A:HOH999 2.0 25.6 1.0
ND1 A:HIS101 2.2 17.4 1.0
OD2 A:ASP128 2.2 12.8 1.0
OD2 A:ASP232 2.2 17.0 1.0
CG A:ASP124 2.9 16.8 1.0
CE1 A:HIS101 3.1 16.1 1.0
CG A:HIS101 3.2 16.2 1.0
CG A:ASP128 3.2 11.6 1.0
CG A:ASP232 3.2 18.5 1.0
MN A:MN514 3.3 18.5 1.0
OD1 A:ASP124 3.4 18.0 1.0
CB A:HIS101 3.6 17.8 1.0
CB A:ASP232 3.6 17.5 1.0
OD1 A:ASP128 3.6 7.8 1.0
CB A:ASP124 4.2 16.9 1.0
NE2 A:HIS101 4.2 14.7 1.0
NE1 A:TRP122 4.3 15.9 1.0
CD2 A:HIS101 4.3 15.4 1.0
OD1 A:ASP232 4.4 14.9 1.0
NZ A:LYS401 4.4 24.7 1.0
O A:HIS141 4.4 17.8 1.0
CZ2 A:TRP122 4.5 17.7 1.0
CB A:ASP128 4.5 12.1 1.0
OE2 A:GLU277 4.6 17.8 1.0
CG A:GLU277 4.7 17.4 1.0
CE A:LYS401 4.7 23.8 1.0
CE2 A:TRP122 4.7 16.0 1.0
ND1 A:HIS126 4.8 14.4 1.0
OD1 A:ASP234 4.9 17.6 1.0
CA A:ASP232 4.9 16.6 1.0

Manganese binding site 3 out of 4 in 3lp4

Go back to Manganese Binding Sites List in 3lp4
Manganese binding site 3 out of 4 in the Crystal Structure of Human Arginase I in Complex with L-Lysine, 1.90A 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 L-Lysine, 1.90A Resolution. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn514

b:18.4
occ:1.00
OD1 B:ASP234 2.0 23.1 1.0
OD1 B:ASP124 2.2 19.6 1.0
O B:HOH350 2.2 20.2 1.0
ND1 B:HIS126 2.3 17.5 1.0
OD2 B:ASP232 2.3 16.2 1.0
OD2 B:ASP234 2.5 22.4 1.0
CG B:ASP234 2.6 23.5 1.0
CG B:ASP124 3.0 17.3 1.0
CG B:ASP232 3.0 16.8 1.0
CE1 B:HIS126 3.0 18.0 1.0
OD2 B:ASP124 3.2 17.5 1.0
MN B:MN515 3.2 19.2 1.0
CG B:HIS126 3.4 18.7 1.0
OD1 B:ASP232 3.5 17.0 1.0
NZ B:LYS402 3.7 30.8 1.0
CB B:HIS126 3.9 17.0 1.0
N B:HIS126 4.0 16.2 1.0
OG1 B:THR246 4.0 24.8 1.0
CB B:ASP232 4.0 17.1 1.0
CB B:ASP234 4.1 20.4 1.0
N B:ALA125 4.2 17.5 1.0
CE B:LYS402 4.2 28.7 1.0
NE2 B:HIS126 4.3 19.0 1.0
CB B:ASP124 4.4 17.3 1.0
CD2 B:HIS126 4.4 18.6 1.0
CA B:HIS126 4.5 17.2 1.0
O B:HOH341 4.5 18.9 1.0
OD1 B:ASP128 4.5 15.8 1.0
OD2 B:ASP128 4.6 14.6 1.0
CD B:LYS402 4.6 27.7 1.0
CB B:ALA125 4.7 13.4 1.0
O B:THR246 4.8 26.2 1.0
C B:ALA125 4.8 15.3 1.0
CA B:ALA125 4.9 15.3 1.0
CA B:ASP124 4.9 16.8 1.0
O B:HIS126 4.9 17.5 1.0
CG B:ASP128 5.0 16.6 1.0

Manganese binding site 4 out of 4 in 3lp4

Go back to Manganese Binding Sites List in 3lp4
Manganese binding site 4 out of 4 in the Crystal Structure of Human Arginase I in Complex with L-Lysine, 1.90A 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 L-Lysine, 1.90A Resolution. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn515

b:19.2
occ:1.00
O B:HOH350 1.8 20.2 1.0
OD2 B:ASP124 2.0 17.5 1.0
OD2 B:ASP128 2.0 14.6 1.0
ND1 B:HIS101 2.2 20.0 1.0
OD2 B:ASP232 2.2 16.2 1.0
CG B:ASP128 3.1 16.6 1.0
CG B:ASP124 3.1 17.3 1.0
CE1 B:HIS101 3.2 19.7 1.0
CG B:HIS101 3.2 20.8 1.0
CG B:ASP232 3.2 16.8 1.0
MN B:MN514 3.2 18.4 1.0
CB B:HIS101 3.5 20.9 1.0
OD1 B:ASP128 3.5 15.8 1.0
OD1 B:ASP124 3.5 19.6 1.0
CB B:ASP232 3.5 17.1 1.0
NZ B:LYS402 4.1 30.8 1.0
NE1 B:TRP122 4.3 13.4 1.0
NE2 B:HIS101 4.3 20.6 1.0
CD2 B:HIS101 4.3 22.7 1.0
CB B:ASP124 4.3 17.3 1.0
CB B:ASP128 4.4 17.1 1.0
OD1 B:ASP232 4.4 17.0 1.0
CZ2 B:TRP122 4.4 15.2 1.0
CE B:LYS402 4.4 28.7 1.0
O B:HIS141 4.6 20.2 1.0
CE2 B:TRP122 4.6 17.2 1.0
CG B:GLU277 4.7 25.6 1.0
O B:HIS126 4.7 17.5 1.0
OD1 B:ASP234 4.8 23.1 1.0
CA B:ASP232 4.9 18.8 1.0
OE2 B:GLU277 4.9 27.9 1.0
ND1 B:HIS126 4.9 17.5 1.0
OD2 B:ASP234 4.9 22.4 1.0
CA B:HIS101 5.0 21.9 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 04:11:55 2020

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