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4Y2X

Structure of soluble epoxide hydrolase in complex with 2-({[2-(adamantan-1-yl)ethyl]amino}methyl)phenol

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0001558biological_processregulation of cell growth
A0003824molecular_functioncatalytic activity
A0004301molecular_functionepoxide hydrolase activity
A0005737cellular_componentcytoplasm
A0005777cellular_componentperoxisome
A0005782cellular_componentperoxisomal matrix
A0005829cellular_componentcytosol
A0006629biological_processlipid metabolic process
A0009056biological_processcatabolic process
A0009636biological_processresponse to toxic substance
A0010628biological_processpositive regulation of gene expression
A0015643molecular_functiontoxic substance binding
A0016311biological_processdephosphorylation
A0016787molecular_functionhydrolase activity
A0016791molecular_functionphosphatase activity
A0033885molecular_function10-hydroxy-9-(phosphonooxy)octadecanoate phosphatase activity
A0042577molecular_functionlipid phosphatase activity
A0042632biological_processcholesterol homeostasis
A0042803molecular_functionprotein homodimerization activity
A0046272biological_processstilbene catabolic process
A0046839biological_processphospholipid dephosphorylation
A0046872molecular_functionmetal ion binding
A0052642molecular_functionlysophosphatidic acid phosphatase activity
A0070062cellular_componentextracellular exosome
A0090181biological_processregulation of cholesterol metabolic process
A0097176biological_processepoxide metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue MG A 601
ChainResidue
AASP9
AASP11
AASP185

site_idAC2
Number of Residues8
Detailsbinding site for residue 4A0 A 602
ChainResidue
AMET419
ATYR466
APHE267
AASP335
ATRP336
ATHR360
ATYR383
AGLN384

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 Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:15096040
ChainResidueDetails
AASP9
AASP11
ATHR123
AASP185

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
ATYR383

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS43

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P34914
ChainResidueDetails
ALYS55
ALYS421
ALYS455
ALYS554

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P34914
ChainResidueDetails
ALYS191
ALYS215

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P34914
ChainResidueDetails
ASER370

site_idSWS_FT_FI10
Number of Residues1
DetailsLIPID: S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine => ECO:0000305|PubMed:21164107
ChainResidueDetails
ACYS522

227111

PDB entries from 2024-11-06

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