6Q39
Complex of Arginase 2 with Example 49
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 | HDQ405 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue MN A 402 |
| Chain | Residue |
| A | ASP253 |
| A | MN401 |
| A | HDQ405 |
| 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 | VAL26 |
| A | LEU61 |
| A | CYS63 |
| A | PHE323 |
| site_id | AC5 |
| Number of Residues | 22 |
| Details | binding site for residue HDQ A 405 |
| Chain | Residue |
| A | HIS120 |
| A | ASP143 |
| A | HIS145 |
| A | ASP147 |
| A | ASN149 |
| A | SER156 |
| A | HIS160 |
| A | ASP200 |
| A | ASP202 |
| A | GLU205 |
| A | ASP251 |
| A | ASP253 |
| A | THR265 |
| A | GLU296 |
| A | MN401 |
| A | MN402 |
| A | HOH521 |
| A | HOH523 |
| A | HOH525 |
| A | HOH546 |
| A | HOH571 |
| A | HOH578 |
| 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 | HDQ405 |
| 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 | HDQ405 |
| 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 | AD1 |
| Number of Residues | 20 |
| Details | binding site for residue HDQ B 405 |
| Chain | Residue |
| B | HIS120 |
| B | ASP143 |
| B | HIS145 |
| B | ASP147 |
| B | ASN149 |
| B | SER156 |
| B | HIS160 |
| B | ASP200 |
| B | ASP202 |
| B | GLU205 |
| B | ASP251 |
| B | ASP253 |
| B | THR265 |
| B | GLU296 |
| B | MN401 |
| B | MN402 |
| B | HOH513 |
| B | HOH515 |
| B | HOH527 |
| B | HOH531 |
| site_id | AD2 |
| 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 | HDQ405 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue MN C 402 |
| Chain | Residue |
| C | MN401 |
| C | HDQ405 |
| C | HIS120 |
| C | ASP143 |
| C | ASP147 |
| C | ASP251 |
| site_id | AD4 |
| 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 | AD5 |
| Number of Residues | 3 |
| Details | binding site for residue BME C 404 |
| Chain | Residue |
| C | LEU61 |
| C | CYS63 |
| C | PHE323 |
| site_id | AD6 |
| Number of Residues | 22 |
| Details | binding site for residue HDQ C 405 |
| Chain | Residue |
| C | HIS120 |
| C | ASP143 |
| C | HIS145 |
| C | ASP147 |
| C | ASN149 |
| C | SER156 |
| C | HIS160 |
| C | ASP200 |
| C | ASP202 |
| C | GLU205 |
| C | ASP251 |
| C | ASP253 |
| C | THR265 |
| C | GLU296 |
| C | MN401 |
| C | MN402 |
| C | HOH508 |
| C | HOH532 |
| C | HOH533 |
| C | HOH544 |
| C | HOH547 |
| C | HOH597 |
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 |
