4JBH
2.2A resolution structure of cobalt and zinc bound thermostable alcohol dehydrogenase from Pyrobaculum aerophilum
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| A | 0030554 | molecular_function | adenyl nucleotide binding |
| A | 0043168 | molecular_function | anion binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051262 | biological_process | protein tetramerization |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| B | 0030554 | molecular_function | adenyl nucleotide binding |
| B | 0043168 | molecular_function | anion binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051262 | biological_process | protein tetramerization |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| C | 0030554 | molecular_function | adenyl nucleotide binding |
| C | 0043168 | molecular_function | anion binding |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051262 | biological_process | protein tetramerization |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| D | 0030554 | molecular_function | adenyl nucleotide binding |
| D | 0043168 | molecular_function | anion binding |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0051262 | biological_process | protein tetramerization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 401 |
| Chain | Residue |
| A | CYS91 |
| A | CYS94 |
| A | CYS97 |
| A | CYS105 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CO A 402 |
| Chain | Residue |
| A | CYS91 |
| A | CYS94 |
| A | CYS97 |
| A | CYS105 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL B 401 |
| Chain | Residue |
| B | ARG323 |
| B | ASN175 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 402 |
| Chain | Residue |
| B | CYS91 |
| B | CYS94 |
| B | CYS97 |
| B | CYS105 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CO B 403 |
| Chain | Residue |
| B | CYS91 |
| B | CYS94 |
| B | CYS97 |
| B | CYS105 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL C 401 |
| Chain | Residue |
| C | PRO40 |
| C | GLY174 |
| C | ASN175 |
| C | ARG323 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 402 |
| Chain | Residue |
| C | CYS91 |
| C | CYS94 |
| C | CYS97 |
| C | CYS105 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CO C 403 |
| Chain | Residue |
| C | CYS91 |
| C | CYS94 |
| C | CYS97 |
| C | CYS105 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL D 401 |
| Chain | Residue |
| D | GLY174 |
| D | ASN175 |
| D | ARG323 |
| D | HOH544 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 402 |
| Chain | Residue |
| D | CYS91 |
| D | CYS94 |
| D | CYS97 |
| D | CYS105 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CO D 403 |
| Chain | Residue |
| D | CYS91 |
| D | CYS94 |
| D | CYS97 |
| D | CYS105 |
