Structure of PDB 2clp Chain E Binding Site BS01

Receptor Information
>2clp Chain E (length=323) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
RPATVLGAMEMGRRMDAPTSAAVTRAFLERGHTEIDTAFVYSEGQSETIL
GGLGLRLGGSDCRVKIDTKAIPLFGNSLKPDSLRFQLETSLKRLQCPRVD
LFYLHMPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCK
SNGWILPTVYQGMYNAITRQVETELFPCLRHFGLRFYAFNPLAGGLLTGK
YKYEDKDGKQPVGRFFGNTWAEMYRNRYWKEHHFEGIALVEKALQAAYGA
SAPSMTSATLRWMYHHSQLQGAHGDAVILGMSSLEQLEQNLAAAEEGPLE
PAVVDAFNQAWHLVAHECPNYFR
Ligand information
Ligand IDNDP
InChIInChI=1S/C21H30N7O17P3/c22-17-12-19(25-7-24-17)28(8-26-12)21-16(44-46(33,34)35)14(30)11(43-21)6-41-48(38,39)45-47(36,37)40-5-10-13(29)15(31)20(42-10)27-3-1-2-9(4-27)18(23)32/h1,3-4,7-8,10-11,13-16,20-21,29-31H,2,5-6H2,(H2,23,32)(H,36,37)(H,38,39)(H2,22,24,25)(H2,33,34,35)/t10-,11-,13-,14-,15-,16-,20-,21-/m1/s1
InChIKeyACFIXJIJDZMPPO-NNYOXOHSSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O)(O)O[P@@](=O)(O)OC[C@@H]4[C@H]([C@H]([C@@H](O4)N5C=CCC(=C5)C(=O)N)O)O)O)OP(=O)(O)O)N
CACTVS 3.341NC(=O)C1=CN(C=CC1)[CH]2O[CH](CO[P](O)(=O)O[P](O)(=O)OC[CH]3O[CH]([CH](O[P](O)(O)=O)[CH]3O)n4cnc5c(N)ncnc45)[CH](O)[CH]2O
CACTVS 3.341NC(=O)C1=CN(C=CC1)[C@@H]2O[C@H](CO[P@@](O)(=O)O[P@](O)(=O)OC[C@H]3O[C@H]([C@H](O[P](O)(O)=O)[C@@H]3O)n4cnc5c(N)ncnc45)[C@@H](O)[C@H]2O
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)OCC4C(C(C(O4)N5C=CCC(=C5)C(=O)N)O)O)O)OP(=O)(O)O)N
FormulaC21 H30 N7 O17 P3
NameNADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
ChEMBLCHEMBL407009
DrugBankDB02338
ZINCZINC000008215411
PDB chain2clp Chain E Residue 1361 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB2clp Crystal Structure of Human Aflatoxin B1 Aldehyde Reductase Member 3
Resolution3.0 Å
Binding residue
(original residue number in PDB)		G44 M46 D73 Y78 K106 H142 S172 N173 Q198 F226 N227 P228 L229 G231 G232 T235 K237 R251 I315 G317 M318 S319 Q323 Q326 N327
Binding residue
(residue number reindexed from 1)		G7 M9 D36 Y41 K69 H105 S135 N136 Q161 F189 N190 P191 L192 G194 G195 T198 K200 R214 I278 G280 M281 S282 Q286 Q289 N290
Annotation score3
Enzymatic activity
Catalytic site (original residue number in PDB) D73 Y78 P109 H142
Catalytic site (residue number reindexed from 1) D36 Y41 P72 H105
Enzyme Commision number 1.-.-.-
Gene Ontology
Molecular Function
GO:0004033 aldo-keto reductase (NADPH) activity
GO:0005515 protein binding
GO:0009055 electron transfer activity
GO:0016491 oxidoreductase activity
GO:0042802 identical protein binding
Biological Process
GO:0006081 cellular aldehyde metabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0005794 Golgi apparatus
GO:0005829 cytosol
GO:0070062 extracellular exosome

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2clp, PDBe:2clp, PDBj:2clp
PDBsum2clp
PubMed
UniProtO95154|ARK73_HUMAN Aflatoxin B1 aldehyde reductase member 3 (Gene Name=AKR7A3)

[Back to BioLiP]