4ZDD

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

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004165	molecular_function	delta(3)-delta(2)-enoyl-CoA isomerase activity
A	0005777	cellular_component	peroxisome
A	0005782	cellular_component	peroxisomal matrix
A	0006631	biological_process	fatty acid metabolic process
A	0006635	biological_process	fatty acid beta-oxidation
A	0016853	molecular_function	isomerase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue SO4 A 300

Chain	Residue
A	ALA70
A	PHE97
A	GLY125
A	LEU126
A	PHE150
A	GLU158

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site_id	AC2
Number of Residues	7
Details	binding site for residue SO4 A 301

Chain	Residue
A	PRO202
A	SER203
A	SER204
A	HOH405
A	ARG64
A	ASN141
A	LYS143

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site_id	AC3
Number of Residues	2
Details	binding site for residue SO4 A 302

Chain	Residue
A	ARG218
A	ARG218

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:26527136

Chain	Residue	Details
A	GLU158

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site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:26527136, ECO:0007744|PDB:4ZDB, ECO:0007744|PDB:4ZDC

Chain	Residue	Details
A	SER68

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site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:26527136, ECO:0007744|PDB:4ZDC

Chain	Residue	Details
A	LEU126

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	4
Details	M-CSA 499

Chain	Residue	Details
A	ALA70	electrostatic stabiliser
A	ASN101	electrostatic stabiliser, modifies pKa
A	LEU126	electrostatic stabiliser
A	GLU158	proton acceptor, proton donor

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