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1ZD2

Human soluble epoxide hydrolase 4-(3-cyclohexyluriedo)-ethanoic acid complex

Functional Information from GO Data
ChainGOidnamespacecontents
P0000287molecular_functionmagnesium ion binding
P0001558biological_processregulation of cell growth
P0003824molecular_functioncatalytic activity
P0004301molecular_functionepoxide hydrolase activity
P0005737cellular_componentcytoplasm
P0005777cellular_componentperoxisome
P0005782cellular_componentperoxisomal matrix
P0005829cellular_componentcytosol
P0006629biological_processlipid metabolic process
P0009636biological_processresponse to toxic substance
P0010628biological_processpositive regulation of gene expression
P0015643molecular_functiontoxic substance binding
P0016311biological_processdephosphorylation
P0016787molecular_functionhydrolase activity
P0016791molecular_functionphosphatase activity
P0033885molecular_function10-hydroxy-9-(phosphonooxy)octadecanoate phosphatase activity
P0042577molecular_functionlipid phosphatase activity
P0042632biological_processcholesterol homeostasis
P0042803molecular_functionprotein homodimerization activity
P0046272biological_processstilbene catabolic process
P0046839biological_processphospholipid dephosphorylation
P0046872molecular_functionmetal ion binding
P0052642molecular_functionlysophosphatidic acid phosphatase activity
P0070062cellular_componentextracellular exosome
P0090181biological_processregulation of cholesterol metabolic process
P0097176biological_processepoxide metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG P 800
ChainResidue
PASP9
PASP11
PASP184
PASP185
PPO4900

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 P 900
ChainResidue
PLYS160
PMG800
PASP9
PASP11
PTHR123
PASN124

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE NC3 P 700
ChainResidue
PPHE265
PASP333
PTRP334
PMET337
PTYR381
PMET418
PTYR465
PVAL497
PHIS523

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues272
DetailsDomain: {"description":"AB hydrolase-1","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"15096040","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16322563","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19746975","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19969453","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20934334","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"15096040","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16322563","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19746975","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19969453","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20934334","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"15096040","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16322563","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19746975","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19969453","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20934334","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15096040","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15096040","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16322563","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19746975","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19969453","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20934334","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues3
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P34914","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P34914","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P34914","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues1
DetailsLipidation: {"description":"S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine","evidences":[{"source":"PubMed","id":"21164107","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1b6g
ChainResidueDetails
PHIS523
PASP495
PASP333

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1b6g
ChainResidueDetails
PTHR123
PLYS160

245663

PDB entries from 2025-12-03

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