7B81
Crystal structure of Azotobacter vinelandii L-rhamnose 1-dehydrogenase (NAD bound-form)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0006633 | biological_process | fatty acid biosynthetic process |
| 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 | 0019301 | biological_process | rhamnose catabolic process |
| A | 0048038 | molecular_function | quinone binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0006633 | biological_process | fatty acid biosynthetic process |
| 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 | 0019301 | biological_process | rhamnose catabolic process |
| B | 0048038 | molecular_function | quinone binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 25 |
| Details | binding site for residue NAD A 301 |
| Chain | Residue |
| A | GLY12 |
| A | ALA94 |
| A | GLY95 |
| A | ILE96 |
| A | THR116 |
| A | VAL144 |
| A | SER145 |
| A | SER146 |
| A | TYR159 |
| A | LYS163 |
| A | PRO189 |
| A | SER14 |
| A | GLY190 |
| A | ILE192 |
| A | THR194 |
| A | ASP195 |
| A | ILE196 |
| A | ASN197 |
| A | ARG15 |
| A | GLY16 |
| A | ILE17 |
| A | ALA65 |
| A | ASP66 |
| A | ALA67 |
| A | ASN93 |
| site_id | AC2 |
| Number of Residues | 26 |
| Details | binding site for residue NAD B 301 |
| Chain | Residue |
| B | GLY12 |
| B | SER14 |
| B | ARG15 |
| B | GLY16 |
| B | ILE17 |
| B | SER37 |
| B | ALA65 |
| B | ASP66 |
| B | ALA67 |
| B | ASN93 |
| B | GLY95 |
| B | ILE96 |
| B | THR116 |
| B | VAL144 |
| B | SER145 |
| B | SER146 |
| B | TYR159 |
| B | LYS163 |
| B | PRO189 |
| B | GLY190 |
| B | ILE192 |
| B | THR194 |
| B | ASP195 |
| B | ILE196 |
| B | ASN197 |
| B | HOH405 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"O93868","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"O93868","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Lowers pKa of active site Tyr","evidences":[{"source":"UniProtKB","id":"O93868","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"33482017","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7B81","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7DO6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7DO7","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"33482017","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7DO6","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"33482017","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7DO7","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
