4IXV
Crystal structure of human Arginase-2 complexed with inhibitor 2d: {(5R)-5-amino-5-carboxy-5-[1-(4-chlorobenzyl)piperidin-4-yl]pentyl}(trihydroxy)borate(1-)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004053 | molecular_function | arginase activity |
A | 0006525 | biological_process | arginine metabolic process |
A | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
A | 0046872 | molecular_function | metal ion binding |
B | 0004053 | molecular_function | arginase activity |
B | 0006525 | biological_process | arginine metabolic process |
B | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
B | 0046872 | molecular_function | metal ion binding |
C | 0004053 | molecular_function | arginase activity |
C | 0006525 | biological_process | arginine metabolic process |
C | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
C | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN A 401 |
Chain | Residue |
A | HIS120 |
A | ASP143 |
A | ASP147 |
A | ASP251 |
A | MN402 |
A | XA1405 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN A 402 |
Chain | Residue |
A | ASP253 |
A | MN401 |
A | XA1405 |
A | ASP143 |
A | HIS145 |
A | ASP251 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE BEN A 403 |
Chain | Residue |
A | ASN83 |
A | ASN83 |
A | ASN84 |
A | LEU85 |
A | PRO151 |
A | LEU152 |
A | THR153 |
A | THR154 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE BME A 404 |
Chain | Residue |
A | LEU61 |
A | CYS63 |
A | HIS284 |
A | PHE323 |
site_id | AC5 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE XA1 A 405 |
Chain | Residue |
A | LYS38 |
A | HIS120 |
A | ASP143 |
A | HIS145 |
A | ASP147 |
A | ASN149 |
A | SER155 |
A | SER156 |
A | HIS160 |
A | ASP202 |
A | ASP251 |
A | ASP253 |
A | THR265 |
A | GLU296 |
A | MN401 |
A | MN402 |
A | HOH516 |
A | HOH558 |
A | HOH559 |
A | HOH573 |
A | HOH574 |
A | HOH599 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN B 401 |
Chain | Residue |
B | HIS120 |
B | ASP143 |
B | ASP147 |
B | ASP251 |
B | MN402 |
B | XA1405 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN B 402 |
Chain | Residue |
B | ASP143 |
B | HIS145 |
B | ASP251 |
B | ASP253 |
B | MN401 |
B | XA1405 |
site_id | AC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE BEN B 403 |
Chain | Residue |
B | ASN83 |
B | ASN83 |
B | ASN84 |
B | LEU85 |
B | PRO151 |
B | LEU152 |
B | THR153 |
B | THR154 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE BME B 404 |
Chain | Residue |
B | LEU61 |
B | CYS63 |
B | PHE323 |
site_id | BC1 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE XA1 B 405 |
Chain | Residue |
B | HIS120 |
B | ASP143 |
B | HIS145 |
B | ASP147 |
B | ASN149 |
B | SER156 |
B | HIS160 |
B | ASP202 |
B | ASP251 |
B | ASP253 |
B | THR265 |
B | GLU296 |
B | MN401 |
B | MN402 |
B | HOH515 |
B | HOH524 |
B | HOH536 |
B | HOH544 |
B | HOH556 |
B | HOH639 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN C 401 |
Chain | Residue |
C | ASP143 |
C | HIS145 |
C | ASP251 |
C | ASP253 |
C | MN402 |
C | XA1405 |
site_id | BC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN C 402 |
Chain | Residue |
C | MN401 |
C | XA1405 |
C | HIS120 |
C | ASP143 |
C | ASP147 |
C | ASP251 |
site_id | BC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE BEN C 403 |
Chain | Residue |
C | ASN83 |
C | ASN83 |
C | ASN84 |
C | LEU85 |
C | PRO151 |
C | LEU152 |
C | THR153 |
C | THR154 |
site_id | BC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE BME C 404 |
Chain | Residue |
C | HIS24 |
C | LEU61 |
C | CYS63 |
C | PHE323 |
site_id | BC6 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE XA1 C 405 |
Chain | Residue |
C | HIS120 |
C | ASP143 |
C | HIS145 |
C | ASP147 |
C | ASN149 |
C | SER155 |
C | SER156 |
C | HIS160 |
C | ASP202 |
C | ASP251 |
C | ASP253 |
C | THR265 |
C | GLU296 |
C | MN401 |
C | MN402 |
C | HOH519 |
C | HOH522 |
C | HOH527 |
C | HOH529 |
C | HOH530 |
C | HOH544 |
C | HOH559 |
Functional Information from PROSITE/UniProt
site_id | PS01053 |
Number of Residues | 22 |
Details | ARGINASE_1 Arginase family signature. SFDIDafdPtlaPAtgtpvvgG |
Chain | Residue | Details |
A | SER249-GLY270 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 27 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12859189, ECO:0007744|PDB:1PQ3, ECO:0007744|PDB:4HZE, ECO:0007744|PDB:4I06, ECO:0007744|PDB:4IE2, ECO:0007744|PDB:4IE3, ECO:0007744|PDB:4IXU, ECO:0007744|PDB:4IXV |
Chain | Residue | Details |
A | HIS120 | |
B | HIS120 | |
B | ASP143 | |
B | HIS145 | |
B | ASP147 | |
B | SER156 | |
B | ASP202 | |
B | ASP251 | |
B | ASP253 | |
B | GLU296 | |
C | HIS120 | |
A | ASP143 | |
C | ASP143 | |
C | HIS145 | |
C | ASP147 | |
C | SER156 | |
C | ASP202 | |
C | ASP251 | |
C | ASP253 | |
C | GLU296 | |
A | HIS145 | |
A | ASP147 | |
A | SER156 | |
A | ASP202 | |
A | ASP251 | |
A | ASP253 | |
A | GLU296 |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P53608 |
Chain | Residue | Details |
A | THR265 | |
B | THR265 | |
C | THR265 |