4ZDF

Crystal structure of yeast enoyl-CoA isomerase helix-10 deletion (ScECI2-H10) mutant

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	binding site for residue GOL A 301

Chain	Residue
A	GLY69
A	ALA70
A	ARG100
A	GLY125
A	LEU126
A	LEU155
A	GLU158

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:26527136

Chain	Residue	Details
A	GLU158
B	GLU158

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site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:26527136, ECO:0007744|PDB:4ZDB, ECO:0007744|PDB:4ZDC

Chain	Residue	Details
A	SER68
B	SER68

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site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:26527136, ECO:0007744|PDB:4ZDC

Chain	Residue	Details
A	LEU126
B	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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site_id	MCSA2
Number of Residues	4
Details	M-CSA 499

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

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