2FPR
Crystal structure the N-terminal domain of E. coli HisB. Apo Mg model.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000105 | biological_process | L-histidine biosynthetic process |
| A | 0004401 | molecular_function | histidinol-phosphatase activity |
| A | 0004424 | molecular_function | imidazoleglycerol-phosphate dehydratase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0016791 | molecular_function | phosphatase activity |
| B | 0000105 | biological_process | L-histidine biosynthetic process |
| B | 0004401 | molecular_function | histidinol-phosphatase activity |
| B | 0004424 | molecular_function | imidazoleglycerol-phosphate dehydratase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0016791 | molecular_function | phosphatase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 501 |
| Chain | Residue |
| B | CYS94 |
| B | HIS96 |
| B | CYS102 |
| B | CYS104 |
| B | ARG105 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 502 |
| Chain | Residue |
| A | ARG105 |
| A | CYS94 |
| A | HIS96 |
| A | CYS102 |
| A | CYS104 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 503 |
| Chain | Residue |
| A | ASP10 |
| A | ASP12 |
| A | ASP131 |
| A | HOH662 |
| A | HOH675 |
| A | HOH683 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 504 |
| Chain | Residue |
| B | ASP10 |
| B | ASP12 |
| B | ASP131 |
| B | HOH772 |
| B | HOH778 |
| B | HOH780 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA B 505 |
| Chain | Residue |
| B | ASP12 |
| B | GLU18 |
| B | PHE23 |
| B | HOH554 |
| B | HOH568 |
| B | HOH584 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE BR A 506 |
| Chain | Residue |
| A | ASP10 |
| A | ASN56 |
| A | LYS106 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE BR B 507 |
| Chain | Residue |
| B | ASP10 |
| B | ASN56 |
| B | LYS106 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE BR A 508 |
| Chain | Residue |
| A | GLN40 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE BR B 509 |
| Chain | Residue |
| A | GLN79 |
| B | PRO20 |
| B | SER21 |
| site_id | BC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE BR B 510 |
| Chain | Residue |
| B | GLN40 |
| site_id | BC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE BR B 511 |
| Chain | Residue |
| A | GLN63 |
| B | ARG148 |
| site_id | BC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE BR A 512 |
| Chain | Residue |
| A | THR82 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"HAMAP-Rule","id":"MF_01022","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16966333","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_01022","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16966333","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01022","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16966333","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
