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8QMZ

Soluble epoxide hydrolase in complex with RK4

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
B0003824molecular_functioncatalytic activity
C0003824molecular_functioncatalytic activity
D0003824molecular_functioncatalytic activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
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
BASP335
CASP335
DASP335

site_idSWS_FT_FI2
Number of Residues4
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
BTYR466
CTYR466
DTYR466

site_idSWS_FT_FI3
Number of Residues4
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
BHIS524
CHIS524
DHIS524

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:15096040, ECO:0000269|PubMed:16322563, ECO:0000269|PubMed:19746975, ECO:0000269|PubMed:19969453, ECO:0000269|PubMed:20934334
ChainResidueDetails
ATYR383
BTYR383
CTYR383
DTYR383

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P34914
ChainResidueDetails
ASER370
BSER370
CSER370
DSER370

site_idSWS_FT_FI6
Number of Residues12
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P34914
ChainResidueDetails
ALYS421
DLYS421
DLYS455
DLYS554
ALYS455
ALYS554
BLYS421
BLYS455
BLYS554
CLYS421
CLYS455
CLYS554

site_idSWS_FT_FI7
Number of Residues4
DetailsLIPID: S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine => ECO:0000305|PubMed:21164107
ChainResidueDetails
ACYS522
BCYS522
CCYS522
DCYS522

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PDB entries from 2024-09-04

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