2FPX
Crystal Structure of the N-terminal Domain of E.coli HisB- Sulfate complex.
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 601 |
| 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 602 |
| 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 603 |
| Chain | Residue |
| A | ASP10 |
| A | ASP12 |
| A | ASP131 |
| A | HOH768 |
| A | HOH794 |
| A | HOH799 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 604 |
| Chain | Residue |
| B | ASP10 |
| B | ASP12 |
| B | ASP131 |
| B | HOH911 |
| B | HOH916 |
| B | HOH921 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 605 |
| Chain | Residue |
| B | HOH692 |
| B | HOH717 |
| B | HOH726 |
| B | HOH727 |
| B | HOH755 |
| B | HOH799 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 B 606 |
| Chain | Residue |
| B | ASN56 |
| B | LYS106 |
| B | ARG132 |
| B | THR134 |
| B | HOH672 |
| B | HOH717 |
| B | HOH730 |
| B | HOH731 |
| B | HOH755 |
| B | HOH799 |
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 |
