5ZEH
Crystal structure of Entamoeba histolytica Arginase in complex with L- Ornithine at 2.35 A
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000050 | biological_process | urea cycle |
| A | 0004053 | molecular_function | arginase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006525 | biological_process | arginine metabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0030145 | molecular_function | manganese ion binding |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0052170 | biological_process | symbiont-mediated suppression of host innate immune response |
| B | 0000050 | biological_process | urea cycle |
| B | 0004053 | molecular_function | arginase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006525 | biological_process | arginine metabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0030145 | molecular_function | manganese ion binding |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0052170 | biological_process | symbiont-mediated suppression of host innate immune response |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | binding site for residue ORN A 301 |
| Chain | Residue |
| A | HIS126 |
| A | ASP128 |
| A | ASN130 |
| A | SER137 |
| A | HIS141 |
| A | ASP178 |
| A | HOH401 |
| A | HOH403 |
| A | HOH406 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue MN A 302 |
| Chain | Residue |
| A | HIS98 |
| A | ASP124 |
| A | ASP128 |
| A | ASP225 |
| A | MN303 |
| A | HOH401 |
| A | HOH406 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue MN A 303 |
| Chain | Residue |
| A | ASP124 |
| A | HIS126 |
| A | ASP225 |
| A | ASP227 |
| A | MN302 |
| A | HOH401 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 304 |
| Chain | Residue |
| A | ASN115 |
| A | ARG117 |
| A | ASP218 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | binding site for residue ORN B 301 |
| Chain | Residue |
| B | HIS126 |
| B | ASP128 |
| B | ASN130 |
| B | SER137 |
| B | HIS141 |
| B | GLY142 |
| B | ASP178 |
| B | HOH402 |
| B | HOH405 |
| B | HOH412 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue MN B 302 |
| Chain | Residue |
| B | HIS98 |
| B | ASP124 |
| B | ASP128 |
| B | ASP225 |
| B | MN303 |
| B | HOH402 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue MN B 303 |
| Chain | Residue |
| B | ASP124 |
| B | HIS126 |
| B | ASP225 |
| B | ASP227 |
| B | MN302 |
| B | HOH402 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"31199070","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5ZEE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5ZEF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5ZEH","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"31199070","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"5ZEE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5ZEF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5ZEH","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
