Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1ZD2

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

Functional Information from GO Data
ChainGOidnamespacecontents
P0000287molecular_functionmagnesium ion binding
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
P0019439biological_processobsolete aromatic compound catabolic process
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 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
PASP333

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
PTYR465

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
PHIS523

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:15096040
ChainResidueDetails
PASP9
PASP11
PASP185
PTHR123

site_idSWS_FT_FI5
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
PTYR381

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
PLYS43

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P34914
ChainResidueDetails
PLYS55
PLYS420
PLYS454
PLYS553

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P34914
ChainResidueDetails
PLYS191
PLYS215

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P34914
ChainResidueDetails
PSER368

site_idSWS_FT_FI10
Number of Residues1
DetailsLIPID: S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine => ECO:0000305|PubMed:21164107
ChainResidueDetails
PCYS521

219869

PDB entries from 2024-05-15

PDB statisticsPDBj update infoContact PDBjnumon