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4C4Y

Crystal structure of human bifunctional epoxide hydroxylase 2 complexed with A4

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 7WI A 1548
ChainResidue
APHE267
ATRP525
AASP335
ATRP336
AMET339
ATYR383
APHE387
ALEU408
ATYR466
AHIS524

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:15096040, ECO:0000269|PubMed:16322563, ECO:0000269|PubMed:19746975, ECO:0000269|PubMed:19969453, ECO:0000269|PubMed:20934334
ChainResidueDetails
AASP335

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:15096040, ECO:0000269|PubMed:16322563, ECO:0000269|PubMed:19746975, ECO:0000269|PubMed:19969453, ECO:0000269|PubMed:20934334
ChainResidueDetails
ATYR466

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:15096040, ECO:0000269|PubMed:16322563, ECO:0000269|PubMed:19746975, ECO:0000269|PubMed:19969453, ECO:0000269|PubMed:20934334
ChainResidueDetails
AHIS524

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:15096040, ECO:0000269|PubMed:16322563, ECO:0000269|PubMed:19746975, ECO:0000269|PubMed:19969453, ECO:0000269|PubMed:20934334
ChainResidueDetails
ATYR383

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P34914
ChainResidueDetails
ASER370

site_idSWS_FT_FI6
Number of Residues3
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P34914
ChainResidueDetails
ALYS421
ALYS455
ALYS554

site_idSWS_FT_FI7
Number of Residues1
DetailsLIPID: S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine => ECO:0000305|PubMed:21164107
ChainResidueDetails
ACYS522

219140

PDB entries from 2024-05-01

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