3MEQ
Crystal structure of alcohol dehydrogenase from Brucella melitensis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
| A | 0008270 | molecular_function | zinc ion 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 | 0046872 | molecular_function | metal ion binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
| B | 0008270 | molecular_function | zinc ion 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 | 0046872 | molecular_function | metal ion binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
| C | 0008270 | molecular_function | zinc ion 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 | 0046872 | molecular_function | metal ion binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
| D | 0008270 | molecular_function | zinc ion 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 | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 401 |
| Chain | Residue |
| A | CYS42 |
| A | HIS65 |
| A | CYS152 |
| A | EDO402 |
| A | NAI601 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO A 402 |
| Chain | Residue |
| A | TRP91 |
| A | CYS152 |
| A | LEU268 |
| A | ZN401 |
| A | NAI601 |
| A | CYS42 |
| A | THR44 |
| A | TRP53 |
| A | HIS65 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 501 |
| Chain | Residue |
| A | CYS96 |
| A | CYS99 |
| A | CYS102 |
| A | CYS110 |
| site_id | AC4 |
| Number of Residues | 36 |
| Details | BINDING SITE FOR RESIDUE NAI A 601 |
| Chain | Residue |
| A | CYS42 |
| A | HIS43 |
| A | THR44 |
| A | HIS47 |
| A | CYS152 |
| A | THR156 |
| A | GLY176 |
| A | ILE177 |
| A | GLY178 |
| A | GLY179 |
| A | LEU180 |
| A | ASP199 |
| A | ILE200 |
| A | LYS204 |
| A | THR243 |
| A | ALA244 |
| A | VAL245 |
| A | SER246 |
| A | ALA249 |
| A | ASN266 |
| A | GLY267 |
| A | LEU268 |
| A | SER290 |
| A | ILE291 |
| A | VAL292 |
| A | ARG337 |
| A | HOH354 |
| A | HOH378 |
| A | ZN401 |
| A | EDO402 |
| A | HOH403 |
| A | HOH464 |
| A | HOH477 |
| A | HOH482 |
| A | HOH551 |
| D | VAL281 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 345 |
| Chain | Residue |
| A | ASP307 |
| A | LYS309 |
| C | ASN194 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL A 346 |
| Chain | Residue |
| A | ARG189 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 347 |
| Chain | Residue |
| A | TYR118 |
| A | HOH390 |
| D | LEU282 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 401 |
| Chain | Residue |
| B | CYS42 |
| B | HIS65 |
| B | CYS152 |
| B | EDO402 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 402 |
| Chain | Residue |
| B | THR44 |
| B | HIS65 |
| B | TRP91 |
| B | CYS152 |
| B | LEU268 |
| B | ILE291 |
| B | ZN401 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 501 |
| Chain | Residue |
| B | CYS96 |
| B | CYS99 |
| B | CYS102 |
| B | CYS110 |
| site_id | BC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO B 345 |
| Chain | Residue |
| B | PRO90 |
| B | TRP91 |
| B | LEU92 |
| B | GLY293 |
| B | THR294 |
| B | LEU298 |
| B | HOH363 |
| B | HOH374 |
| B | HOH409 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 346 |
| Chain | Residue |
| B | THR108 |
| B | LEU109 |
| B | SER290 |
| B | ILE291 |
| C | VAL281 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 347 |
| Chain | Residue |
| B | VAL41 |
| B | ARG337 |
| B | ILE338 |
| site_id | BC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 348 |
| Chain | Residue |
| B | LEU161 |
| B | THR166 |
| B | MET191 |
| B | HOH352 |
| B | HOH460 |
| D | PRO168 |
| site_id | BC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO B 349 |
| Chain | Residue |
| B | GLN26 |
| B | GLN33 |
| site_id | BC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 350 |
| Chain | Residue |
| B | GLY169 |
| B | ASN194 |
| D | PHE304 |
| D | ASP307 |
| D | LYS309 |
| D | HOH373 |
| site_id | BC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 351 |
| Chain | Residue |
| A | LYS140 |
| A | ASN141 |
| A | ASP143 |
| B | ARG86 |
| B | LYS140 |
| B | ASN141 |
| B | ASP143 |
| site_id | BC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 401 |
| Chain | Residue |
| C | CYS42 |
| C | HIS65 |
| C | CYS152 |
| C | EDO402 |
| site_id | CC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO C 402 |
| Chain | Residue |
| C | THR44 |
| C | HIS65 |
| C | TRP91 |
| C | CYS152 |
| C | LEU268 |
| C | ZN401 |
| site_id | CC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 501 |
| Chain | Residue |
| C | CYS96 |
| C | CYS99 |
| C | CYS102 |
| C | CYS110 |
| site_id | CC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL C 345 |
| Chain | Residue |
| C | ARG210 |
| site_id | CC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO C 346 |
| Chain | Residue |
| A | ASN194 |
| C | ASP303 |
| C | PHE304 |
| C | ASP307 |
| C | HOH371 |
| site_id | CC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NA C 347 |
| Chain | Residue |
| C | ASN121 |
| C | VAL129 |
| site_id | CC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 401 |
| Chain | Residue |
| D | CYS42 |
| D | HIS65 |
| D | CYS152 |
| D | EDO402 |
| site_id | CC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO D 402 |
| Chain | Residue |
| D | CYS42 |
| D | THR44 |
| D | HIS65 |
| D | TRP91 |
| D | CYS152 |
| D | LEU268 |
| D | ILE291 |
| D | VAL292 |
| D | ZN401 |
| site_id | CC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 501 |
| Chain | Residue |
| D | CYS96 |
| D | CYS99 |
| D | CYS102 |
| D | CYS110 |
| site_id | CC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO D 345 |
| Chain | Residue |
| D | LEU254 |
| D | ASN279 |
| D | ASN283 |
| D | HOH374 |
| D | HOH487 |
| D | HOH521 |
| site_id | DC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO D 346 |
| Chain | Residue |
| D | VAL41 |
| D | HIS43 |
| D | GLY336 |
| D | ARG337 |
| D | ILE338 |
| site_id | DC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO D 347 |
| Chain | Residue |
| A | VAL281 |
| D | THR108 |
| D | SER290 |
| D | ILE291 |
| D | VAL292 |
Functional Information from PROSITE/UniProt
| site_id | PS00059 |
| Number of Residues | 15 |
| Details | ADH_ZINC Zinc-containing alcohol dehydrogenases signature. GHEgVGFvsavGsgV |
| Chain | Residue | Details |
| A | GLY64-VAL78 |
