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5AKI

ligand complex structure of soluble epoxide hydrolase

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
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 Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 1549
ChainResidue
ALYS144
APHE147

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 1550
ChainResidue
AALA365
ATRP473
AALA476
AHOH2248
AHOH2297

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 1551
ChainResidue
ATYR466
AMET469
AASN472
AHOH2295
AHOH2297
AHOH2366
ATRP336
AGLN384

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 1552
ChainResidue
AILE305
AGLU306
AARG467
AARG471
AHOH2256

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 1553
ChainResidue
AGLY44
ALYS191
AASP195

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PEG A 1554
ChainResidue
APHE149
ATHR172

site_idAC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE PEG A 1555
ChainResidue
AGLN505

site_idAC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PEG A 1556
ChainResidue
AGLN107
AMET111
AGLN220
ATHR224
APRO225
APRO227
AHOH2073
AHOH2076
AHOH2083

site_idAC9
Number of Residues1
DetailsBINDING SITE FOR RESIDUE DMS A 1557
ChainResidue
AHOH2169

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE 6NF A 1558
ChainResidue
APHE267
AASP335
ATYR383
AGLN384
AMET419
ATYR466

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

238895

PDB entries from 2025-07-16

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