2FPS
Crystal structure of the N-terminal domain of E.coli HisB- Apo Ca 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 CA A 503 |
| Chain | Residue |
| A | ASP10 |
| A | ASP12 |
| A | ASP131 |
| A | HOH509 |
| A | HOH528 |
| A | HOH529 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 504 |
| Chain | Residue |
| B | ASP10 |
| B | ASP12 |
| B | ASP131 |
| B | HOH515 |
| B | HOH527 |
| B | HOH539 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 505 |
| Chain | Residue |
| A | ASP10 |
| A | ASN56 |
| A | LYS106 |
| A | HOH581 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 506 |
| Chain | Residue |
| B | ASP10 |
| B | ASN56 |
| B | LYS106 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_01022, ECO:0000305|PubMed:16966333 |
| Chain | Residue | Details |
| A | ASP10 | |
| B | ASP10 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_01022, ECO:0000305|PubMed:16966333 |
| Chain | Residue | Details |
| A | ASP12 | |
| B | ASP12 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 14 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01022, ECO:0000269|PubMed:16966333 |
| Chain | Residue | Details |
| A | ASP10 | |
| B | CYS94 | |
| B | HIS96 | |
| B | CYS102 | |
| B | CYS104 | |
| B | ASP131 | |
| A | ASP12 | |
| A | CYS94 | |
| A | HIS96 | |
| A | CYS102 | |
| A | CYS104 | |
| A | ASP131 | |
| B | ASP10 | |
| B | ASP12 |
