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4ZDD

Structure of yeast D3,D2-enoyl-CoA isomerase bound to sulphate ion

Functional Information from GO Data
ChainGOidnamespacecontents
A0004165molecular_functiondelta(3)-delta(2)-enoyl-CoA isomerase activity
A0005777cellular_componentperoxisome
A0005782cellular_componentperoxisomal matrix
A0006629biological_processlipid metabolic process
A0006631biological_processfatty acid metabolic process
A0006635biological_processfatty acid beta-oxidation
A0016853molecular_functionisomerase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue SO4 A 300
ChainResidue
AALA70
APHE97
AGLY125
ALEU126
APHE150
AGLU158

site_idAC2
Number of Residues7
Detailsbinding site for residue SO4 A 301
ChainResidue
APRO202
ASER203
ASER204
AHOH405
AARG64
AASN141
ALYS143

site_idAC3
Number of Residues2
Detailsbinding site for residue SO4 A 302
ChainResidue
AARG218
AARG218

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"26527136","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"26527136","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4ZDB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ZDC","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"26527136","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4ZDC","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 499
ChainResidueDetails
AALA70electrostatic stabiliser
AASN101electrostatic stabiliser, modifies pKa
ALEU126electrostatic stabiliser
AGLU158proton acceptor, proton donor

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PDB entries from 2025-07-23

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