7DO7
Crystal structure of Azotobacter vinelandii L-rhamnose 1-dehydrogenase(NAD and L-rhamnose 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 | 0019299 | biological_process | rhamnose metabolic process |
| 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 | 0019299 | biological_process | rhamnose metabolic process |
| B | 0019301 | biological_process | rhamnose catabolic process |
| B | 0048038 | molecular_function | quinone binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 33 |
| Details | binding site for residue NAD A 301 |
| Chain | Residue |
| A | GLY12 |
| A | ASN93 |
| A | ALA94 |
| A | GLY95 |
| A | THR116 |
| A | VAL144 |
| A | SER145 |
| A | SER146 |
| A | TYR159 |
| A | LYS163 |
| A | PRO189 |
| A | SER14 |
| A | GLY190 |
| A | THR191 |
| A | ILE192 |
| A | THR194 |
| A | ASP195 |
| A | ILE196 |
| A | ASN197 |
| A | RM4302 |
| A | HOH413 |
| A | HOH426 |
| A | ARG15 |
| A | HOH428 |
| A | HOH437 |
| A | HOH440 |
| A | HOH523 |
| A | GLY16 |
| A | ILE17 |
| A | SER37 |
| A | ALA65 |
| A | ASP66 |
| A | ALA67 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | binding site for residue RM4 A 302 |
| Chain | Residue |
| A | PHE99 |
| A | SER146 |
| A | SER148 |
| A | GLN156 |
| A | TYR159 |
| A | THR191 |
| A | ASN197 |
| A | GLN256 |
| A | NAD301 |
| A | HOH425 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue RM4 A 303 |
| Chain | Residue |
| A | ASP235 |
| A | MET236 |
| A | ARG238 |
| B | ASP223 |
| B | GLY227 |
| B | HOH421 |
| B | HOH423 |
| site_id | AC4 |
| Number of Residues | 33 |
| 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 | ALA94 |
| B | GLY95 |
| B | ILE96 |
| B | VAL144 |
| B | SER145 |
| B | SER146 |
| B | TYR159 |
| B | LYS163 |
| B | PRO189 |
| B | GLY190 |
| B | THR191 |
| B | ILE192 |
| B | THR194 |
| B | ASP195 |
| B | ILE196 |
| B | ASN197 |
| B | RM4302 |
| B | HOH417 |
| B | HOH434 |
| B | HOH440 |
| B | HOH483 |
| B | HOH493 |
| B | HOH494 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | binding site for residue RM4 B 302 |
| Chain | Residue |
| B | PHE99 |
| B | SER146 |
| B | SER148 |
| B | GLN156 |
| B | TYR159 |
| B | THR191 |
| B | ILE196 |
| B | ASN197 |
| B | GLN256 |
| B | NAD301 |
| B | HOH422 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue RM4 B 303 |
| Chain | Residue |
| B | HOH451 |
| B | HOH516 |
| A | ASP223 |
| A | GLY227 |
| B | ASP235 |
| B | MET236 |
| B | ARG238 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000250|UniProtKB:O93868 |
| Chain | Residue | Details |
| A | SER146 | |
| B | SER146 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:O93868 |
| Chain | Residue | Details |
| A | TYR159 | |
| B | TYR159 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | ACT_SITE: Lowers pKa of active site Tyr => ECO:0000250|UniProtKB:O93868 |
| Chain | Residue | Details |
| A | LYS163 | |
| B | LYS163 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 20 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:33482017, ECO:0007744|PDB:7B81, ECO:0007744|PDB:7DO6, ECO:0007744|PDB:7DO7 |
| Chain | Residue | Details |
| A | GLY12 | |
| A | ILE192 | |
| B | GLY12 | |
| B | SER14 | |
| B | ARG15 | |
| B | ILE17 | |
| B | ASP66 | |
| B | ALA67 | |
| B | ASN93 | |
| B | TYR159 | |
| B | LYS163 | |
| A | SER14 | |
| B | ILE192 | |
| A | ARG15 | |
| A | ILE17 | |
| A | ASP66 | |
| A | ALA67 | |
| A | ASN93 | |
| A | TYR159 | |
| A | LYS163 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:33482017, ECO:0007744|PDB:7DO6 |
| Chain | Residue | Details |
| A | SER37 | |
| B | SER37 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:33482017, ECO:0007744|PDB:7DO7 |
| Chain | Residue | Details |
| A | SER146 | |
| B | ASN197 | |
| A | SER148 | |
| A | GLN156 | |
| A | THR191 | |
| A | ASN197 | |
| B | SER146 | |
| B | SER148 | |
| B | GLN156 | |
| B | THR191 |
