Structure of PDB 1o01 Chain C Binding Site BS02

Receptor Information
>1o01 Chain C (length=495) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
QAVPAPNQQPEVFCNQIFINNEWHDAVSRKTFPTVNPSTGEVICQVAEGD
KEDVDKAVKAARAAFQLGSPWRRMDASHRGRLLNRLADLIERDRTYLAAL
ETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTR
HEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVA
NLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGRVIQV
AAGSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAG
SRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGPQVDETQFKKILG
YINTGKQEGAKLLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVM
QILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNC
YDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTVKVPQKNS
Ligand information
Ligand IDNAD
InChIInChI=1S/C21H27N7O14P2/c22-17-12-19(25-7-24-17)28(8-26-12)21-16(32)14(30)11(41-21)6-39-44(36,37)42-43(34,35)38-5-10-13(29)15(31)20(40-10)27-3-1-2-9(4-27)18(23)33/h1-4,7-8,10-11,13-16,20-21,29-32H,5-6H2,(H5-,22,23,24,25,33,34,35,36,37)/t10-,11-,13-,14-,15-,16-,20-,21-/m1/s1
InChIKeyBAWFJGJZGIEFAR-NNYOXOHSSA-N
SMILES
SoftwareSMILES
CACTVS 3.341NC(=O)c1ccc[n+](c1)[C@@H]2O[C@H](CO[P]([O-])(=O)O[P@](O)(=O)OC[C@H]3O[C@H]([C@H](O)[C@@H]3O)n4cnc5c(N)ncnc45)[C@@H](O)[C@H]2O
OpenEye OEToolkits 1.5.0c1cc(c[n+](c1)C2C(C(C(O2)COP(=O)([O-])OP(=O)(O)OCC3C(C(C(O3)n4cnc5c4ncnc5N)O)O)O)O)C(=O)N
CACTVS 3.341NC(=O)c1ccc[n+](c1)[CH]2O[CH](CO[P]([O-])(=O)O[P](O)(=O)OC[CH]3O[CH]([CH](O)[CH]3O)n4cnc5c(N)ncnc45)[CH](O)[CH]2O
OpenEye OEToolkits 1.5.0c1cc(c[n+](c1)[C@H]2[C@@H]([C@@H]([C@H](O2)CO[P@@](=O)([O-])O[P@@](=O)(O)OC[C@@H]3[C@H]([C@H]([C@@H](O3)n4cnc5c4ncnc5N)O)O)O)O)C(=O)N
FormulaC21 H27 N7 O14 P2
NameNICOTINAMIDE-ADENINE-DINUCLEOTIDE
ChEMBLCHEMBL1234613
DrugBankDB14128
ZINC
PDB chain1o01 Chain C Residue 5503 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1o01 Coenzyme isomerization is integral to catalysis in aldehyde dehydrogenase
Resolution2.15 Å
Binding residue
(original residue number in PDB)		I165 I166 P167 W168 K192 E195 G225 G229 A230 F243 G245 S246 I249 L269 C302 Q349 E399 F401
Binding residue
(residue number reindexed from 1)		I160 I161 P162 W163 K187 E190 G220 G224 A225 F238 G240 S241 I244 L264 C297 Q344 E394 F396
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) N169 K192 E268 C302 E399 E476
Catalytic site (residue number reindexed from 1) N164 K187 E263 C297 E394 E471
Enzyme Commision number 1.2.1.3: aldehyde dehydrogenase (NAD(+)).
Gene Ontology
Molecular Function
GO:0004029 aldehyde dehydrogenase (NAD+) activity
GO:0004030 aldehyde dehydrogenase [NAD(P)+] activity
GO:0008957 phenylacetaldehyde dehydrogenase (NAD+) activity
GO:0009055 electron transfer activity
GO:0016491 oxidoreductase activity
GO:0016620 oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
GO:0051287 NAD binding
GO:0106435 carboxylesterase activity
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006066 alcohol metabolic process
GO:0006068 ethanol catabolic process
GO:0018937 nitroglycerin metabolic process
GO:0046185 aldehyde catabolic process
GO:1903179 regulation of dopamine biosynthetic process
GO:1905627 regulation of serotonin biosynthetic process
Cellular Component
GO:0005739 mitochondrion
GO:0005759 mitochondrial matrix
GO:0070062 extracellular exosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1o01, PDBe:1o01, PDBj:1o01
PDBsum1o01
PubMed12795606
UniProtP05091|ALDH2_HUMAN Aldehyde dehydrogenase, mitochondrial (Gene Name=ALDH2)

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