4IXU
Crystal structure of human Arginase-2 complexed with inhibitor 11d: {(5R)-5-amino-5-carboxy-5-[(3-endo)-8-(3,4-dichlorobenzyl)-8-azabicyclo[3.2.1]oct-3-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 | 38I406 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN A 402 |
| Chain | Residue |
| A | ASP253 |
| A | MN401 |
| A | 38I406 |
| 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 | 2 |
| Details | BINDING SITE FOR RESIDUE BME A 404 |
| Chain | Residue |
| A | LEU58 |
| A | PHE323 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE BME A 405 |
| Chain | Residue |
| A | HIS133 |
| A | CYS134 |
| A | SER290 |
| site_id | AC6 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE 38I A 406 |
| Chain | Residue |
| A | LEU81 |
| 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 | HOH503 |
| A | HOH526 |
| A | HOH531 |
| A | HOH544 |
| A | HOH643 |
| A | HOH659 |
| A | HOH671 |
| 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 | 38I406 |
| 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 | 38I406 |
| 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 | 2 |
| Details | BINDING SITE FOR RESIDUE BME B 404 |
| Chain | Residue |
| B | CYS63 |
| B | PHE323 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE BME B 405 |
| Chain | Residue |
| A | ASP136 |
| B | CYS134 |
| B | HOH552 |
| B | HOH568 |
| B | HOH767 |
| site_id | BC3 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE 38I B 406 |
| Chain | Residue |
| B | LEU81 |
| B | HIS120 |
| B | ASP143 |
| B | HIS145 |
| B | ASP147 |
| B | ASN149 |
| B | SER155 |
| B | SER156 |
| B | HIS160 |
| B | ASP202 |
| B | ASP251 |
| B | ASP253 |
| B | THR265 |
| B | GLU296 |
| B | MN401 |
| B | MN402 |
| B | HOH502 |
| B | HOH505 |
| B | HOH532 |
| B | HOH533 |
| B | HOH548 |
| B | HOH677 |
| B | HOH689 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN C 401 |
| Chain | Residue |
| C | ASP251 |
| C | ASP253 |
| C | MN402 |
| C | 38I406 |
| C | ASP143 |
| C | HIS145 |
| site_id | BC5 |
| 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 | 38I406 |
| site_id | BC6 |
| 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 | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE BME C 404 |
| Chain | Residue |
| C | HIS24 |
| C | VAL26 |
| C | LEU58 |
| C | CYS63 |
| C | PHE323 |
| site_id | BC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BME C 405 |
| Chain | Residue |
| C | VAL107 |
| C | HIS130 |
| C | HIS133 |
| C | PRO135 |
| site_id | BC9 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE 38I C 406 |
| Chain | Residue |
| C | LEU81 |
| 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 | HOH501 |
| C | HOH513 |
| C | HOH522 |
| C | HOH539 |
| C | HOH602 |
| C | HOH633 |
| C | HOH634 |
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 |
