4IE2
Crystal structure of human Arginase-2 complexed with inhibitor 1h
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 | 1EC405 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN A 402 |
| Chain | Residue |
| A | ASP253 |
| A | MN401 |
| A | 1EC405 |
| A | ASP143 |
| A | HIS145 |
| A | ASP251 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE BEN A 403 |
| Chain | Residue |
| A | ASN83 |
| A | ASN83 |
| A | ASN84 |
| A | LEU85 |
| A | PRO151 |
| A | LEU152 |
| A | THR154 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE BME A 404 |
| Chain | Residue |
| A | HIS24 |
| A | HIS284 |
| A | PHE323 |
| A | BME406 |
| A | HOH607 |
| A | HOH614 |
| A | HOH663 |
| site_id | AC5 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE 1EC A 405 |
| Chain | Residue |
| A | HIS120 |
| A | ASP143 |
| A | HIS145 |
| A | ASP147 |
| A | ASN149 |
| A | SER156 |
| A | HIS160 |
| A | ASP202 |
| A | ASP251 |
| A | ASP253 |
| A | THR265 |
| A | GLU296 |
| A | MN401 |
| A | MN402 |
| A | HOH502 |
| A | HOH512 |
| A | HOH521 |
| A | HOH522 |
| A | HOH555 |
| A | HOH556 |
| A | HOH674 |
| A | HOH709 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BME A 406 |
| Chain | Residue |
| A | LEU61 |
| A | GLY62 |
| A | PHE323 |
| A | BME404 |
| site_id | AC7 |
| 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 | 1EC406 |
| site_id | AC8 |
| 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 | 1EC406 |
| site_id | AC9 |
| 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 | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE BME B 404 |
| Chain | Residue |
| B | HIS24 |
| B | LEU61 |
| B | CYS63 |
| B | HIS284 |
| B | PHE323 |
| B | BME407 |
| B | HOH669 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE BME B 405 |
| Chain | Residue |
| A | PRO135 |
| A | ARG169 |
| B | HIS133 |
| B | CYS134 |
| B | PRO135 |
| B | ASP136 |
| B | PRO245 |
| site_id | BC3 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE 1EC B 406 |
| Chain | Residue |
| B | GLU296 |
| B | MN401 |
| B | MN402 |
| B | HOH507 |
| B | HOH511 |
| B | HOH521 |
| B | HOH531 |
| B | HOH536 |
| B | HOH715 |
| B | HIS120 |
| B | ASP143 |
| B | HIS145 |
| B | ASP147 |
| B | ASN149 |
| B | SER155 |
| B | SER156 |
| B | HIS160 |
| B | GLY161 |
| B | ASP202 |
| B | ASP251 |
| B | ASP253 |
| B | THR265 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE BME B 407 |
| Chain | Residue |
| B | VAL26 |
| B | LEU61 |
| B | GLY62 |
| B | PHE323 |
| B | BME404 |
| site_id | BC5 |
| 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 | 1EC404 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN C 402 |
| Chain | Residue |
| C | HIS120 |
| C | ASP143 |
| C | ASP147 |
| C | ASP251 |
| C | MN401 |
| C | 1EC404 |
| site_id | BC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE BEN C 403 |
| Chain | Residue |
| C | ASN83 |
| C | ASN83 |
| C | ASN84 |
| C | LEU85 |
| C | LEU85 |
| C | PRO151 |
| C | LEU152 |
| C | THR154 |
| site_id | BC8 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE 1EC C 404 |
| Chain | Residue |
| C | HIS120 |
| C | ASP143 |
| C | HIS145 |
| C | ASP147 |
| C | ASN149 |
| C | SER156 |
| C | HIS160 |
| C | ASP202 |
| C | ASP251 |
| C | ASP253 |
| C | THR265 |
| C | GLU296 |
| C | MN401 |
| C | MN402 |
| C | HOH513 |
| C | HOH514 |
| C | HOH519 |
| C | HOH522 |
| C | HOH556 |
| C | HOH617 |
| site_id | BC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BME C 405 |
| Chain | Residue |
| C | HIS24 |
| C | CYS63 |
| C | HIS284 |
| C | PHE323 |
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 | ASP251 | |
| A | ASP253 | |
| A | GLU296 | |
| B | HIS120 | |
| B | ASP143 | |
| B | HIS145 | |
| B | ASP147 | |
| B | SER156 | |
| B | ASP202 | |
| B | ASP251 | |
| B | ASP253 | |
| B | GLU296 | |
| C | HIS120 | |
| C | ASP143 | |
| C | HIS145 | |
| C | ASP147 | |
| C | SER156 | |
| C | ASP202 | |
| C | ASP251 | |
| C | ASP253 | |
| C | GLU296 | |
| A | HIS120 | |
| A | ASP143 | |
| A | HIS145 | |
| A | ASP147 | |
| A | SER156 | |
| A | ASP202 |
| 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 |
