1D1S
WILD-TYPE HUMAN SIGMA (CLASS IV) ALCOHOL DEHYDROGENASE
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0001523 | biological_process | retinoid metabolic process |
A | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
A | 0004031 | molecular_function | aldehyde oxidase activity |
A | 0004745 | molecular_function | all-trans-retinol dehydrogenase (NAD+) activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0005886 | cellular_component | plasma membrane |
A | 0006629 | biological_process | lipid metabolic process |
A | 0008270 | molecular_function | zinc ion binding |
A | 0009617 | biological_process | response to bacterium |
A | 0010430 | biological_process | fatty acid omega-oxidation |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0019841 | molecular_function | retinol binding |
A | 0035276 | molecular_function | ethanol binding |
A | 0042572 | biological_process | retinol metabolic process |
A | 0042573 | biological_process | retinoic acid metabolic process |
A | 0045471 | biological_process | response to ethanol |
A | 0046872 | molecular_function | metal ion binding |
A | 0048019 | molecular_function | receptor antagonist activity |
A | 0050153 | molecular_function | omega-hydroxydecanoate dehydrogenase activity |
B | 0001523 | biological_process | retinoid metabolic process |
B | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
B | 0004031 | molecular_function | aldehyde oxidase activity |
B | 0004745 | molecular_function | all-trans-retinol dehydrogenase (NAD+) activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0005886 | cellular_component | plasma membrane |
B | 0006629 | biological_process | lipid metabolic process |
B | 0008270 | molecular_function | zinc ion binding |
B | 0009617 | biological_process | response to bacterium |
B | 0010430 | biological_process | fatty acid omega-oxidation |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0019841 | molecular_function | retinol binding |
B | 0035276 | molecular_function | ethanol binding |
B | 0042572 | biological_process | retinol metabolic process |
B | 0042573 | biological_process | retinoic acid metabolic process |
B | 0045471 | biological_process | response to ethanol |
B | 0046872 | molecular_function | metal ion binding |
B | 0048019 | molecular_function | receptor antagonist activity |
B | 0050153 | molecular_function | omega-hydroxydecanoate dehydrogenase activity |
C | 0001523 | biological_process | retinoid metabolic process |
C | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
C | 0004031 | molecular_function | aldehyde oxidase activity |
C | 0004745 | molecular_function | all-trans-retinol dehydrogenase (NAD+) activity |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0005886 | cellular_component | plasma membrane |
C | 0006629 | biological_process | lipid metabolic process |
C | 0008270 | molecular_function | zinc ion binding |
C | 0009617 | biological_process | response to bacterium |
C | 0010430 | biological_process | fatty acid omega-oxidation |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0019841 | molecular_function | retinol binding |
C | 0035276 | molecular_function | ethanol binding |
C | 0042572 | biological_process | retinol metabolic process |
C | 0042573 | biological_process | retinoic acid metabolic process |
C | 0045471 | biological_process | response to ethanol |
C | 0046872 | molecular_function | metal ion binding |
C | 0048019 | molecular_function | receptor antagonist activity |
C | 0050153 | molecular_function | omega-hydroxydecanoate dehydrogenase activity |
D | 0001523 | biological_process | retinoid metabolic process |
D | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
D | 0004031 | molecular_function | aldehyde oxidase activity |
D | 0004745 | molecular_function | all-trans-retinol dehydrogenase (NAD+) activity |
D | 0005737 | cellular_component | cytoplasm |
D | 0005829 | cellular_component | cytosol |
D | 0005886 | cellular_component | plasma membrane |
D | 0006629 | biological_process | lipid metabolic process |
D | 0008270 | molecular_function | zinc ion binding |
D | 0009617 | biological_process | response to bacterium |
D | 0010430 | biological_process | fatty acid omega-oxidation |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0019841 | molecular_function | retinol binding |
D | 0035276 | molecular_function | ethanol binding |
D | 0042572 | biological_process | retinol metabolic process |
D | 0042573 | biological_process | retinoic acid metabolic process |
D | 0045471 | biological_process | response to ethanol |
D | 0046872 | molecular_function | metal ion binding |
D | 0048019 | molecular_function | receptor antagonist activity |
D | 0050153 | molecular_function | omega-hydroxydecanoate dehydrogenase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 375 |
Chain | Residue |
A | CYS97 |
A | CYS100 |
A | CYS103 |
A | CYS111 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 376 |
Chain | Residue |
A | CYS46 |
A | HIS67 |
A | CYS174 |
A | ACT501 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN D 375 |
Chain | Residue |
D | CYS100 |
D | CYS103 |
D | CYS111 |
D | CYS97 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN D 376 |
Chain | Residue |
D | CYS46 |
D | HIS67 |
D | CYS174 |
D | ACT511 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 375 |
Chain | Residue |
B | CYS97 |
B | CYS100 |
B | CYS103 |
B | CYS111 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN B 376 |
Chain | Residue |
B | CYS46 |
B | HIS67 |
B | CYS174 |
B | ACT506 |
B | NAD2377 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN C 375 |
Chain | Residue |
C | CYS97 |
C | CYS100 |
C | CYS103 |
C | CYS111 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN C 376 |
Chain | Residue |
C | CYS46 |
C | HIS67 |
C | CYS174 |
C | ACT505 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 401 |
Chain | Residue |
A | HIS271 |
A | ACT504 |
A | HOH749 |
A | NAD1377 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ZN A 402 |
Chain | Residue |
A | HIS138 |
A | ACT502 |
A | ACT513 |
site_id | BC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 403 |
Chain | Residue |
B | HIS271 |
B | ACT507 |
B | HOH735 |
B | NAD2377 |
site_id | BC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 404 |
Chain | Residue |
B | HIS138 |
B | HOH725 |
D | GLU357 |
D | GLU360 |
site_id | BC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 405 |
Chain | Residue |
B | ASP341 |
D | GLU99 |
D | ACT508 |
D | ACT509 |
site_id | BC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 406 |
Chain | Residue |
B | GLU16 |
B | CAC551 |
B | CAC552 |
B | CAC553 |
site_id | BC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN C 407 |
Chain | Residue |
C | HIS271 |
C | ACT510 |
C | HOH771 |
C | NAD3377 |
site_id | BC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 408 |
Chain | Residue |
A | GLU357 |
A | GLU360 |
A | HOH793 |
C | HIS138 |
site_id | BC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN D 409 |
Chain | Residue |
D | HIS271 |
D | ACT512 |
D | HOH780 |
D | NAD4377 |
site_id | BC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN D 410 |
Chain | Residue |
D | HIS138 |
D | ACT514 |
D | HOH693 |
D | HOH867 |
site_id | CC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN D 411 |
Chain | Residue |
B | CAC551 |
B | CAC552 |
B | CAC553 |
D | HIS348 |
site_id | CC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ACT A 501 |
Chain | Residue |
A | THR48 |
A | PHE93 |
A | VAL294 |
A | ZN376 |
A | HOH916 |
A | NAD1377 |
site_id | CC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACT A 502 |
Chain | Residue |
A | LYS60 |
A | VAL122 |
A | HIS138 |
A | ZN402 |
A | ACT513 |
site_id | CC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ACT A 504 |
Chain | Residue |
A | HIS271 |
A | ZN401 |
A | NAD1377 |
site_id | CC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE ACT C 505 |
Chain | Residue |
C | CYS46 |
C | THR48 |
C | HIS67 |
C | PHE93 |
C | MET141 |
C | CYS174 |
C | ZN376 |
C | HOH956 |
C | NAD3377 |
site_id | CC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE ACT B 506 |
Chain | Residue |
B | CYS46 |
B | THR48 |
B | PHE93 |
B | MET141 |
B | CYS174 |
B | ZN376 |
B | HOH933 |
B | NAD2377 |
site_id | CC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACT B 507 |
Chain | Residue |
A | ZN403 |
B | LEU224 |
B | HIS271 |
B | HOH735 |
B | NAD2377 |
site_id | CC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ACT D 508 |
Chain | Residue |
B | ZN405 |
D | GLU99 |
D | ARG113 |
D | ACT509 |
site_id | CC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACT D 509 |
Chain | Residue |
B | ASP341 |
B | ZN405 |
D | LYS34 |
D | GLU99 |
D | ACT508 |
site_id | DC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ACT C 510 |
Chain | Residue |
C | HIS271 |
C | ZN407 |
C | NAD3377 |
site_id | DC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE ACT D 511 |
Chain | Residue |
D | CYS46 |
D | THR48 |
D | HIS67 |
D | PHE93 |
D | CYS174 |
D | ZN376 |
D | HOH977 |
D | NAD4377 |
site_id | DC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ACT D 512 |
Chain | Residue |
D | HIS271 |
D | ZN409 |
D | HOH780 |
D | HOH1013 |
site_id | DC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ACT A 513 |
Chain | Residue |
A | HIS138 |
A | ZN402 |
A | ACT502 |
site_id | DC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ACT D 514 |
Chain | Residue |
D | HIS138 |
D | ZN410 |
D | HOH693 |
site_id | DC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE CAC B 551 |
Chain | Residue |
B | GLU16 |
B | PHE61 |
B | ZN406 |
B | CAC552 |
B | CAC553 |
D | HIS348 |
D | GLN366 |
D | ZN411 |
site_id | DC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CAC B 552 |
Chain | Residue |
B | GLU16 |
B | ZN406 |
B | CAC551 |
B | CAC553 |
D | HIS348 |
D | ZN411 |
site_id | DC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CAC B 553 |
Chain | Residue |
B | GLU16 |
B | ZN406 |
B | CAC551 |
B | CAC552 |
B | HOH903 |
D | HIS348 |
D | ZN411 |
site_id | DC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CAC A 554 |
Chain | Residue |
A | MET233 |
A | ALA237 |
A | HOH889 |
site_id | EC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CAC B 555 |
Chain | Residue |
A | GLY259 |
A | ASN260 |
B | ASN101 |
B | ILE112 |
B | HOH613 |
B | HOH622 |
site_id | EC2 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE NAD A 1377 |
Chain | Residue |
A | ARG47 |
A | THR48 |
A | HIS51 |
A | CYS174 |
A | THR178 |
A | GLY201 |
A | GLY202 |
A | VAL203 |
A | ASP223 |
A | LEU224 |
A | LYS228 |
A | VAL268 |
A | ILE269 |
A | HIS271 |
A | VAL292 |
A | GLY293 |
A | VAL294 |
A | CYS317 |
A | PHE319 |
A | ARG369 |
A | ZN401 |
A | ACT501 |
A | ACT504 |
A | HOH623 |
A | HOH888 |
A | HOH901 |
A | HOH911 |
B | PHE309 |
site_id | EC3 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE NAD B 2377 |
Chain | Residue |
A | PHE309 |
A | ZN403 |
B | ARG47 |
B | THR48 |
B | HIS51 |
B | CYS174 |
B | THR178 |
B | GLY201 |
B | GLY202 |
B | VAL203 |
B | ASP223 |
B | LEU224 |
B | LYS228 |
B | ILE269 |
B | HIS271 |
B | VAL292 |
B | GLY293 |
B | VAL294 |
B | CYS317 |
B | VAL318 |
B | PHE319 |
B | ARG369 |
B | ZN376 |
B | ACT506 |
B | ACT507 |
B | HOH697 |
B | HOH897 |
B | HOH900 |
site_id | EC4 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE NAD C 3377 |
Chain | Residue |
C | ARG47 |
C | THR48 |
C | HIS51 |
C | CYS174 |
C | THR178 |
C | GLY201 |
C | GLY202 |
C | VAL203 |
C | ASP223 |
C | LEU224 |
C | LYS228 |
C | VAL268 |
C | ILE269 |
C | HIS271 |
C | VAL292 |
C | GLY293 |
C | VAL294 |
C | CYS317 |
C | PHE319 |
C | ARG369 |
C | ZN407 |
C | ACT505 |
C | ACT510 |
C | HOH770 |
C | HOH771 |
C | HOH845 |
D | PHE309 |
site_id | EC5 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE NAD D 4377 |
Chain | Residue |
D | ARG47 |
D | THR48 |
D | HIS51 |
D | CYS174 |
D | THR178 |
D | GLY201 |
D | GLY202 |
D | VAL203 |
D | ASP223 |
D | LEU224 |
D | LYS228 |
D | VAL268 |
D | ILE269 |
D | HIS271 |
D | VAL292 |
D | GLY293 |
D | VAL294 |
D | CYS317 |
D | PHE319 |
D | ARG369 |
D | ZN409 |
D | ACT511 |
D | HOH737 |
D | HOH978 |
Functional Information from PROSITE/UniProt
site_id | PS00059 |
Number of Residues | 15 |
Details | ADH_ZINC Zinc-containing alcohol dehydrogenases signature. GHEaTGIvesiGegV |
Chain | Residue | Details |
A | GLY66-VAL80 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 60 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10631979, ECO:0007744|PDB:1AGN, ECO:0007744|PDB:1D1S, ECO:0007744|PDB:1D1T |
Chain | Residue | Details |
A | SER59 | |
A | GLY236 | |
A | ILE241 | |
A | CYS282 | |
A | PRO305 | |
A | LYS330 | |
A | ARG369 | |
B | SER59 | |
B | LYS60 | |
B | VAL80 | |
B | LEU110 | |
A | LYS60 | |
B | ARG113 | |
B | ILE116 | |
B | ASP125 | |
B | GLY187 | |
B | LYS212 | |
B | GLY236 | |
B | ILE241 | |
B | CYS282 | |
B | PRO305 | |
B | LYS330 | |
A | VAL80 | |
B | ARG369 | |
C | SER59 | |
C | LYS60 | |
C | VAL80 | |
C | LEU110 | |
C | ARG113 | |
C | ILE116 | |
C | ASP125 | |
C | GLY187 | |
C | LYS212 | |
A | LEU110 | |
C | GLY236 | |
C | ILE241 | |
C | CYS282 | |
C | PRO305 | |
C | LYS330 | |
C | ARG369 | |
D | SER59 | |
D | LYS60 | |
D | VAL80 | |
D | LEU110 | |
A | ARG113 | |
D | ARG113 | |
D | ILE116 | |
D | ASP125 | |
D | GLY187 | |
D | LYS212 | |
D | GLY236 | |
D | ILE241 | |
D | CYS282 | |
D | PRO305 | |
D | LYS330 | |
A | ILE116 | |
D | ARG369 | |
A | ASP125 | |
A | GLY187 | |
A | LYS212 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1teh |
Chain | Residue | Details |
A | THR48 | |
A | ARG47 |
site_id | CSA10 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1teh |
Chain | Residue | Details |
B | MET57 |
site_id | CSA11 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1teh |
Chain | Residue | Details |
C | MET57 |
site_id | CSA12 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1teh |
Chain | Residue | Details |
D | MET57 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1teh |
Chain | Residue | Details |
B | THR48 | |
B | ARG47 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1teh |
Chain | Residue | Details |
C | THR48 | |
C | ARG47 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1teh |
Chain | Residue | Details |
D | THR48 | |
D | ARG47 |
site_id | CSA5 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1teh |
Chain | Residue | Details |
A | THR48 | |
A | HIS51 |
site_id | CSA6 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1teh |
Chain | Residue | Details |
B | THR48 | |
B | HIS51 |
site_id | CSA7 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1teh |
Chain | Residue | Details |
C | THR48 | |
C | HIS51 |
site_id | CSA8 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1teh |
Chain | Residue | Details |
D | THR48 | |
D | HIS51 |
site_id | CSA9 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1teh |
Chain | Residue | Details |
A | MET57 |