6Q37
Complex of Arginase 2 with Example 23
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 | HE8405 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue MN A 402 |
| Chain | Residue |
| A | ASP253 |
| A | MN401 |
| A | HE8405 |
| 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 | CYS63 |
| A | PHE323 |
| A | HOH685 |
| site_id | AC5 |
| Number of Residues | 23 |
| Details | binding site for residue HE8 A 405 |
| Chain | Residue |
| A | HIS120 |
| A | ASP143 |
| A | HIS145 |
| A | ASP147 |
| A | ASN149 |
| A | SER156 |
| A | HIS160 |
| A | GLY161 |
| A | ASP202 |
| A | GLU205 |
| A | ASP251 |
| A | ASP253 |
| A | THR265 |
| A | GLU296 |
| A | MN401 |
| A | MN402 |
| A | HOH505 |
| A | HOH523 |
| A | HOH533 |
| A | HOH545 |
| A | HOH585 |
| A | HOH602 |
| A | HOH760 |
| 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 | HE8405 |
| 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 | HE8405 |
| 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 | 4 |
| Details | binding site for residue BME B 404 |
| Chain | Residue |
| B | VAL26 |
| B | CYS63 |
| B | HIS284 |
| B | PHE323 |
| site_id | AD1 |
| Number of Residues | 23 |
| Details | binding site for residue HE8 B 405 |
| Chain | Residue |
| B | HIS120 |
| B | ASP143 |
| B | HIS145 |
| B | ASP147 |
| B | ASN149 |
| B | SER156 |
| B | HIS160 |
| B | GLY161 |
| B | ASP202 |
| B | GLU205 |
| B | ASP251 |
| B | ASP253 |
| B | THR265 |
| B | GLU296 |
| B | MN401 |
| B | MN402 |
| B | HOH526 |
| B | HOH528 |
| B | HOH542 |
| B | HOH546 |
| B | HOH564 |
| B | HOH575 |
| B | HOH680 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue MN C 401 |
| Chain | Residue |
| C | HE8406 |
| C | ASP143 |
| C | HIS145 |
| C | ASP251 |
| C | ASP253 |
| C | MN402 |
| site_id | AD3 |
| 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 | HE8406 |
| 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 | 4 |
| Details | binding site for residue BME C 404 |
| Chain | Residue |
| C | LEU58 |
| C | LEU61 |
| C | CYS63 |
| C | PHE323 |
| site_id | AD6 |
| Number of Residues | 4 |
| Details | binding site for residue EDO C 405 |
| Chain | Residue |
| C | HOH503 |
| C | HOH666 |
| C | HOH687 |
| C | HOH711 |
| site_id | AD7 |
| Number of Residues | 22 |
| Details | binding site for residue HE8 C 406 |
| Chain | Residue |
| C | HIS120 |
| C | ASP143 |
| C | HIS145 |
| C | ASP147 |
| C | ASN149 |
| C | SER156 |
| C | HIS160 |
| C | GLY161 |
| C | ASP202 |
| C | GLU205 |
| C | ASP251 |
| C | ASP253 |
| C | THR265 |
| C | GLU296 |
| C | MN401 |
| C | MN402 |
| C | HOH513 |
| C | HOH520 |
| C | HOH529 |
| C | HOH532 |
| C | HOH570 |
| C | HOH614 |
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 | 42 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12859189","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1PQ3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4HZE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4I06","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4IE2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4IE3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4IXU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4IXV","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P53608","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
