1OJ7
STRUCTURAL GENOMICS, UNKNOWN FUNCTION CRYSTAL STRUCTURE OF E. COLI K-12 YQHD
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000302 | biological_process | response to reactive oxygen species |
A | 0005829 | cellular_component | cytosol |
A | 0008106 | molecular_function | alcohol dehydrogenase (NADP+) 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 | 0018455 | molecular_function | alcohol dehydrogenase [NAD(P)+] activity |
A | 0042802 | molecular_function | identical protein binding |
A | 0046872 | molecular_function | metal ion binding |
A | 1990002 | molecular_function | methylglyoxal reductase (NADPH) (acetol producing) activity |
A | 1990362 | molecular_function | butanol dehydrogenase (NAD+) activity |
B | 0000302 | biological_process | response to reactive oxygen species |
B | 0005829 | cellular_component | cytosol |
B | 0008106 | molecular_function | alcohol dehydrogenase (NADP+) 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 | 0018455 | molecular_function | alcohol dehydrogenase [NAD(P)+] activity |
B | 0042802 | molecular_function | identical protein binding |
B | 0046872 | molecular_function | metal ion binding |
B | 1990002 | molecular_function | methylglyoxal reductase (NADPH) (acetol producing) activity |
B | 1990362 | molecular_function | butanol dehydrogenase (NAD+) activity |
C | 0000302 | biological_process | response to reactive oxygen species |
C | 0005829 | cellular_component | cytosol |
C | 0008106 | molecular_function | alcohol dehydrogenase (NADP+) 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 | 0018455 | molecular_function | alcohol dehydrogenase [NAD(P)+] activity |
C | 0042802 | molecular_function | identical protein binding |
C | 0046872 | molecular_function | metal ion binding |
C | 1990002 | molecular_function | methylglyoxal reductase (NADPH) (acetol producing) activity |
C | 1990362 | molecular_function | butanol dehydrogenase (NAD+) activity |
D | 0000302 | biological_process | response to reactive oxygen species |
D | 0005829 | cellular_component | cytosol |
D | 0008106 | molecular_function | alcohol dehydrogenase (NADP+) 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 | 0018455 | molecular_function | alcohol dehydrogenase [NAD(P)+] activity |
D | 0042802 | molecular_function | identical protein binding |
D | 0046872 | molecular_function | metal ion binding |
D | 1990002 | molecular_function | methylglyoxal reductase (NADPH) (acetol producing) activity |
D | 1990362 | molecular_function | butanol dehydrogenase (NAD+) activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN B1389 |
Chain | Residue |
B | ASP194 |
B | HIS198 |
B | HIS267 |
B | HIS281 |
B | NZQ1388 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN C1388 |
Chain | Residue |
C | BO31390 |
C | ASP194 |
C | HIS198 |
C | HIS267 |
C | HIS281 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL C1389 |
Chain | Residue |
C | GLY38 |
C | GLY39 |
C | SER40 |
C | HOH2031 |
C | HOH2064 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN D1389 |
Chain | Residue |
D | ASP194 |
D | HIS198 |
D | HIS267 |
D | HIS281 |
D | LEU285 |
D | NZQ1388 |
site_id | AC5 |
Number of Residues | 44 |
Details | BINDING SITE FOR RESIDUE NZQ A1388 |
Chain | Residue |
A | GLY38 |
A | GLY39 |
A | SER40 |
A | PRO67 |
A | ASN68 |
A | GLY94 |
A | GLY95 |
A | SER96 |
A | ASP99 |
A | THR138 |
A | LEU139 |
A | ALA141 |
A | THR142 |
A | SER144 |
A | ASN147 |
A | GLY149 |
A | VAL151 |
A | LYS160 |
A | TYR179 |
A | THR182 |
A | LEU183 |
A | GLN187 |
A | ASP194 |
A | HIS198 |
A | HIS267 |
A | HIS271 |
A | HIS281 |
A | HOH2069 |
A | HOH2134 |
A | HOH2170 |
A | HOH2352 |
A | HOH2353 |
A | HOH2354 |
A | HOH2355 |
A | HOH2356 |
A | HOH2357 |
A | HOH2358 |
A | HOH2359 |
A | HOH2360 |
A | HOH2361 |
A | HOH2362 |
A | HOH2363 |
A | HOH2364 |
A | HOH2365 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE BO3 A1389 |
Chain | Residue |
A | ARG186 |
A | ASN190 |
A | ASP280 |
A | GLN283 |
A | GLY338 |
A | VAL339 |
site_id | AC7 |
Number of Residues | 46 |
Details | BINDING SITE FOR RESIDUE NZQ B1388 |
Chain | Residue |
B | HIS281 |
B | ZN1389 |
B | HOH2083 |
B | HOH2161 |
B | HOH2171 |
B | HOH2210 |
B | HOH2417 |
B | HOH2418 |
B | HOH2419 |
B | HOH2420 |
B | HOH2421 |
B | HOH2422 |
B | HOH2423 |
B | HOH2424 |
B | HOH2425 |
B | HOH2426 |
B | HOH2427 |
B | HOH2428 |
B | GLY38 |
B | GLY39 |
B | SER40 |
B | PRO67 |
B | ASN68 |
B | GLY94 |
B | GLY95 |
B | SER96 |
B | ASP99 |
B | THR138 |
B | LEU139 |
B | ALA141 |
B | THR142 |
B | SER144 |
B | ASN147 |
B | GLY149 |
B | VAL151 |
B | LYS160 |
B | TYR179 |
B | THR182 |
B | LEU183 |
B | PRO184 |
B | GLN187 |
B | ASP194 |
B | HIS198 |
B | LEU252 |
B | HIS267 |
B | HIS271 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE BO3 C1390 |
Chain | Residue |
C | ASP194 |
C | HIS198 |
C | HIS267 |
C | HIS281 |
C | ZN1388 |
site_id | AC9 |
Number of Residues | 43 |
Details | BINDING SITE FOR RESIDUE NZQ D1388 |
Chain | Residue |
D | GLY38 |
D | GLY39 |
D | SER40 |
D | PRO67 |
D | ASN68 |
D | GLY94 |
D | GLY95 |
D | SER96 |
D | ASP99 |
D | THR138 |
D | LEU139 |
D | ALA141 |
D | THR142 |
D | SER144 |
D | ASN147 |
D | GLY149 |
D | VAL151 |
D | LYS160 |
D | TYR179 |
D | THR182 |
D | LEU183 |
D | GLN187 |
D | ASP194 |
D | HIS198 |
D | HIS267 |
D | HIS271 |
D | HIS281 |
D | ZN1389 |
D | HOH2090 |
D | HOH2282 |
D | HOH2283 |
D | HOH2284 |
D | HOH2285 |
D | HOH2286 |
D | HOH2287 |
D | HOH2288 |
D | HOH2289 |
D | HOH2290 |
D | HOH2292 |
D | HOH2293 |
D | HOH2294 |
D | HOH2295 |
D | HOH2296 |
Functional Information from PROSITE/UniProt
site_id | PS00060 |
Number of Residues | 21 |
Details | ADH_IRON_2 Iron-containing alcohol dehydrogenases signature 2. WaTHmlGHeLTAmhgLdHAqT |
Chain | Residue | Details |
A | TRP264-THR284 |
site_id | PS00913 |
Number of Residues | 29 |
Details | ADH_IRON_1 Iron-containing alcohol dehydrogenases signature 1. AVlDpvytytlPprqvAnGvvDAFvhtvE |
Chain | Residue | Details |
A | ALA173-GLU201 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 24 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15327949 |
Chain | Residue | Details |
A | GLY38 | |
B | ASN147 | |
B | LYS160 | |
B | TYR179 | |
C | GLY38 | |
C | GLY93 | |
C | THR138 | |
C | ASN147 | |
C | LYS160 | |
C | TYR179 | |
D | GLY38 | |
A | GLY93 | |
D | GLY93 | |
D | THR138 | |
D | ASN147 | |
D | LYS160 | |
D | TYR179 | |
A | THR138 | |
A | ASN147 | |
A | LYS160 | |
A | TYR179 | |
B | GLY38 | |
B | GLY93 | |
B | THR138 |
site_id | SWS_FT_FI2 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15327949, ECO:0007744|PDB:1OJ7 |
Chain | Residue | Details |
A | ASP194 | |
C | HIS198 | |
C | HIS267 | |
C | HIS281 | |
D | ASP194 | |
D | HIS198 | |
D | HIS267 | |
D | HIS281 | |
A | HIS198 | |
A | HIS267 | |
A | HIS281 | |
B | ASP194 | |
B | HIS198 | |
B | HIS267 | |
B | HIS281 | |
C | ASP194 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1dqs |
Chain | Residue | Details |
A | HIS271 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1dqs |
Chain | Residue | Details |
B | HIS271 |
site_id | CSA3 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1dqs |
Chain | Residue | Details |
C | HIS271 |
site_id | CSA4 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1dqs |
Chain | Residue | Details |
D | HIS271 |