2FPW
Crystal Structure of the N-terminal Domain of E.coli HisB- Phosphoaspartate intermediate.
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 | PHD10 |
A | ASP12 |
A | ASP131 |
A | HOH505 |
A | HOH514 |
A | HOH565 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA B 504 |
Chain | Residue |
B | ASP12 |
B | PHE23 |
B | HOH528 |
B | HOH531 |
B | HOH540 |
B | HOH571 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA B 505 |
Chain | Residue |
B | PHD10 |
B | ASP12 |
B | ASP131 |
B | HOH514 |
B | HOH529 |
B | HOH543 |
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 | PHD10 | |
B | PHD10 |
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 | PHD10 | |
B | CYS94 | |
B | HIS96 | |
B | CYS102 | |
B | CYS104 | |
B | ASP131 | |
A | ASP12 | |
A | CYS94 | |
A | HIS96 | |
A | CYS102 | |
A | CYS104 | |
A | ASP131 | |
B | PHD10 | |
B | ASP12 |