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 | 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 | 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 | 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 | 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 |