2HF8
Crystal structure of HypB from Methanocaldococcus jannaschii in the triphosphate form, in complex with zinc
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003924 | molecular_function | GTPase activity |
| A | 0005525 | molecular_function | GTP binding |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016151 | molecular_function | nickel cation binding |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051604 | biological_process | protein maturation |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003924 | molecular_function | GTPase activity |
| B | 0005525 | molecular_function | GTP binding |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0016151 | molecular_function | nickel cation binding |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051604 | biological_process | protein maturation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 301 |
| Chain | Residue |
| A | THR47 |
| A | ASP75 |
| A | GLU120 |
| A | GSP300 |
| A | HOH468 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 301 |
| Chain | Residue |
| B | HOH437 |
| B | THR47 |
| B | ASP75 |
| B | GLU120 |
| B | GSP300 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 401 |
| Chain | Residue |
| A | CYS95 |
| A | CYS127 |
| B | CYS95 |
| B | ZN402 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 402 |
| Chain | Residue |
| A | ZN401 |
| B | CYS95 |
| B | HIS96 |
| B | CYS127 |
| B | HOH462 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 403 |
| Chain | Residue |
| A | HIS100 |
| A | HIS104 |
| B | HIS100 |
| B | HIS104 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 404 |
| Chain | Residue |
| A | HIS100 |
| A | HIS104 |
| B | HIS100 |
| B | HIS104 |
| site_id | AC7 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE GSP A 300 |
| Chain | Residue |
| A | GLY43 |
| A | SER44 |
| A | GLY45 |
| A | LYS46 |
| A | THR47 |
| A | LEU48 |
| A | ASP75 |
| A | ARG78 |
| A | GLU120 |
| A | ASN167 |
| A | LYS168 |
| A | ASP170 |
| A | SER199 |
| A | LEU200 |
| A | LYS201 |
| A | MG301 |
| A | HOH416 |
| A | HOH458 |
| A | HOH464 |
| A | HOH465 |
| A | HOH468 |
| B | GLU146 |
| B | LYS153 |
| B | ALA174 |
| B | VAL175 |
| site_id | AC8 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE GSP B 300 |
| Chain | Residue |
| A | GLU146 |
| A | LYS153 |
| A | ALA174 |
| A | VAL175 |
| B | ILE42 |
| B | GLY43 |
| B | SER44 |
| B | GLY45 |
| B | LYS46 |
| B | THR47 |
| B | LEU48 |
| B | ASP75 |
| B | ARG78 |
| B | GLU120 |
| B | ASN167 |
| B | LYS168 |
| B | ASP170 |
| B | LEU171 |
| B | SER199 |
| B | LEU200 |
| B | LYS201 |
| B | MG301 |
| B | HOH422 |
| B | HOH437 |
| B | HOH453 |
| B | HOH463 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16807243","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2HF8","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16807243","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2HF8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2HF9","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
