1CWN

CRYSTAL STRUCTURE OF PORCINE ALDEHYDE REDUCTASE HOLOENZYME

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Functional Information from GO Data

ChainGOidnamespacecontents
A0005829cellular_componentcytosol
A0008106molecular_functionalcohol dehydrogenase (NADP+) activity
A0004032molecular_functionalditol:NADP+ 1-oxidoreductase activity
A0016491molecular_functionoxidoreductase activity
A0046185biological_processaldehyde catabolic process
A0110095biological_processcellular detoxification of aldehyde
A0042840biological_processD-glucuronate catabolic process
A0019853biological_processL-ascorbic acid biosynthetic process
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Functional Information from PDB Data

site_idNumber of ResiduesDetails
AC17BINDING SITE FOR RESIDUE NAP A 350
ChainResidue
AGLY20
ATRP22
ASER211
ALEU213
ASER215
APRO262
ASER264

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Functional Information from PDB atom coordinates for the "HETATM" binding sites

site_idNumber of ResiduesDetails
NAP_1cwn_A_35018NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE binding site
ChainResidueligand
AGLY20-TRP22NAP: NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
AASP45NAP: NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
ATYR210-SER215NAP: NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
AASP217NAP: NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
AALA246NAP: NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
APRO262-THR266NAP: NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
AARG269NAP: NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE

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Functional Information from PROSITE/UniProt

site_idNumber of ResiduesDetails
PS0006218Aldo/keto reductase family signature 2. [LIVMFY]-x(8)-{L}-[KREQ]-{K}-[LIVM]-G-[LIVM]-[SC]-N-[FY]
ChainResidueDetails
ALEU147-PHE164

PS0006316Aldo/keto reductase family putative active site signature. [LIVM]-[PAIV]-[KR]-[ST]-{EPQG}-{RFI}-x(2)-R-{SVAF}-x-[GSTAEQK]-[NSL]-x
ChainResidueDetails
AILE261-VAL276

PS0079818Aldo/keto reductase family signature 1. G-[FY]-R-[HSAL]-[LIVMF]-D-[STAGCL]-[AS]-x(5)-[EQ]-x(2)-[LIVMCA]-[GS]
ChainResidueDetails
AGLY40-GLY57

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Functional Information from SwissProt/UniProt

site_idNumber of ResiduesDetails
SWS_FT_FI11Proton donor.
ChainResidueDetails
ATYR49

SWS_FT_FI21Substrate.
ChainResidueDetails
AHIS112

SWS_FT_FI31Lowers pKa of active site Tyr (By similarity).
ChainResidueDetails
ALYS79

SWS_FT_FI410NADP (Potential).
ChainResidueDetails
AGLY10-GLY19

SWS_FT_FI563NADP.
ChainResidueDetails
ASER210-ASN272

extCATRES12Mapped from 2alr to 1cwn using BLAST. All catalytic residues present. Original details record follows: a catalytic site defined by CATRES, Medline 92320300, 94250245, 96022988, 97439701, 98284006
ChainResidueDetails
ALYS79activates water, cofactor or residue. stabilises Y49
ATYR49acid/base. donates proton to substrate

CSA14Annotated By Reference To The Literature 1mrq
ChainResidueDetails
ALYS80
AHIS113
AASP45
ATYR50

CSA22Annotated By Reference To The Literature 1mrq
ChainResidueDetails
ALYS80
ATYR50

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Catalytic Information from CSA

site_idNumber of ResiduesDetails
CSA14Annotated By Reference To The Literature 1mrq
ChainResidueDetails
ALYS80
AHIS113
AASP45
ATYR50

CSA22Annotated By Reference To The Literature 1mrq
ChainResidueDetails
ALYS80
ATYR50