1SG4

Crystal structure of human mitochondrial delta3-delta2-enoyl-CoA isomerase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
B	0003824	molecular_function	catalytic activity
C	0003824	molecular_function	catalytic activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	16
Details	BINDING SITE FOR RESIDUE CO8 B 701

Chain	Residue
B	PRO24
B	GLY111
B	ASN135
B	ILE142
B	TYR251
B	LEU255
B	LYS256
B	LYS259
B	VAL25
B	VAL61
B	ALA64
B	LEU66
B	ASP67
B	LEU68
B	PRO109
B	ALA110

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Functional Information from PROSITE/UniProt

site_id	PS00166
Number of Residues	21
Details	ENOYL_COA_HYDRATASE Enoyl-CoA hydratase/isomerase signature. VSaINGacpAGGclvaLtCDY

Chain	Residue	Details
A	VAL101-TYR121

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	9
Details	BINDING: BINDING => ECO:0000269|PubMed:15351645, ECO:0007744|PDB:1SG4

Chain	Residue	Details
A	ALA64
A	GLY111
A	ASN135
B	ALA64
B	GLY111
B	ASN135
C	ALA64
C	GLY111
C	ASN135

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site_id	SWS_FT_FI2
Number of Residues	3
Details	SITE: Important for catalytic activity => ECO:0000305|PubMed:15351645

Chain	Residue	Details
A	GLU136
B	GLU136
C	GLU136

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site_id	SWS_FT_FI3
Number of Residues	6
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P42125

Chain	Residue	Details
A	LYS19
A	LYS241
B	LYS19
B	LYS241
C	LYS19
C	LYS241

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site_id	SWS_FT_FI4
Number of Residues	6
Details	MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P42125

Chain	Residue	Details
A	LYS42
A	LYS246
B	LYS42
B	LYS246
C	LYS42
C	LYS246

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site_id	SWS_FT_FI5
Number of Residues	3
Details	MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861

Chain	Residue	Details
A	LYS47
B	LYS47
C	LYS47

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1dci

Chain	Residue	Details
A	GLU136
A	PRO144

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site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1dci

Chain	Residue	Details
B	GLU136
B	PRO144

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site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1dci

Chain	Residue	Details
C	GLU136
C	PRO144

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site_id	MCSA1
Number of Residues	4
Details	M-CSA 341

Chain	Residue	Details
A	LEU66	electrostatic stabiliser, hydrogen bond donor
A	GLY111	electrostatic stabiliser, hydrogen bond donor
A	ASN135	electrostatic stabiliser, modifies pKa
A	GLU136	polar/non-polar interaction, proton acceptor, proton donor

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site_id	MCSA2
Number of Residues	4
Details	M-CSA 341

Chain	Residue	Details
B	LEU66	electrostatic stabiliser, hydrogen bond donor
B	GLY111	electrostatic stabiliser, hydrogen bond donor
B	ASN135	electrostatic stabiliser, modifies pKa
B	GLU136	polar/non-polar interaction, proton acceptor, proton donor

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site_id	MCSA3
Number of Residues	4
Details	M-CSA 341

Chain	Residue	Details
C	LEU66	electrostatic stabiliser, hydrogen bond donor
C	GLY111	electrostatic stabiliser, hydrogen bond donor
C	ASN135	electrostatic stabiliser, modifies pKa
C	GLU136	polar/non-polar interaction, proton acceptor, proton donor

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