Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2HW5

The crystal structure of human enoyl-coenzyme A (CoA) hydratase short chain 1, ECHS1

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004165	molecular_function	delta(3)-delta(2)-enoyl-CoA isomerase activity
A	0004300	molecular_function	enoyl-CoA hydratase activity
A	0005515	molecular_function	protein binding
A	0005739	cellular_component	mitochondrion
A	0005759	cellular_component	mitochondrial matrix
A	0006629	biological_process	lipid metabolic process
A	0006631	biological_process	fatty acid metabolic process
A	0006635	biological_process	fatty acid beta-oxidation
A	0009083	biological_process	branched-chain amino acid catabolic process
A	0016829	molecular_function	lyase activity
A	0016853	molecular_function	isomerase activity
A	0018812	molecular_function	3-hydroxyacyl-CoA dehydratase activity
A	0043956	molecular_function	3-hydroxypropionyl-CoA dehydratase activity
A	0120092	molecular_function	(2E)-butenoyl-CoA hydratase activity
B	0003824	molecular_function	catalytic activity
B	0004165	molecular_function	delta(3)-delta(2)-enoyl-CoA isomerase activity
B	0004300	molecular_function	enoyl-CoA hydratase activity
B	0005515	molecular_function	protein binding
B	0005739	cellular_component	mitochondrion
B	0005759	cellular_component	mitochondrial matrix
B	0006629	biological_process	lipid metabolic process
B	0006631	biological_process	fatty acid metabolic process
B	0006635	biological_process	fatty acid beta-oxidation
B	0009083	biological_process	branched-chain amino acid catabolic process
B	0016829	molecular_function	lyase activity
B	0016853	molecular_function	isomerase activity
B	0018812	molecular_function	3-hydroxyacyl-CoA dehydratase activity
B	0043956	molecular_function	3-hydroxypropionyl-CoA dehydratase activity
B	0120092	molecular_function	(2E)-butenoyl-CoA hydratase activity
C	0003824	molecular_function	catalytic activity
C	0004165	molecular_function	delta(3)-delta(2)-enoyl-CoA isomerase activity
C	0004300	molecular_function	enoyl-CoA hydratase activity
C	0005515	molecular_function	protein binding
C	0005739	cellular_component	mitochondrion
C	0005759	cellular_component	mitochondrial matrix
C	0006629	biological_process	lipid metabolic process
C	0006631	biological_process	fatty acid metabolic process
C	0006635	biological_process	fatty acid beta-oxidation
C	0009083	biological_process	branched-chain amino acid catabolic process
C	0016829	molecular_function	lyase activity
C	0016853	molecular_function	isomerase activity
C	0018812	molecular_function	3-hydroxyacyl-CoA dehydratase activity
C	0043956	molecular_function	3-hydroxypropionyl-CoA dehydratase activity
C	0120092	molecular_function	(2E)-butenoyl-CoA hydratase activity
D	0003824	molecular_function	catalytic activity
D	0004165	molecular_function	delta(3)-delta(2)-enoyl-CoA isomerase activity
D	0004300	molecular_function	enoyl-CoA hydratase activity
D	0005515	molecular_function	protein binding
D	0005739	cellular_component	mitochondrion
D	0005759	cellular_component	mitochondrial matrix
D	0006629	biological_process	lipid metabolic process
D	0006631	biological_process	fatty acid metabolic process
D	0006635	biological_process	fatty acid beta-oxidation
D	0009083	biological_process	branched-chain amino acid catabolic process
D	0016829	molecular_function	lyase activity
D	0016853	molecular_function	isomerase activity
D	0018812	molecular_function	3-hydroxyacyl-CoA dehydratase activity
D	0043956	molecular_function	3-hydroxypropionyl-CoA dehydratase activity
D	0120092	molecular_function	(2E)-butenoyl-CoA hydratase activity
E	0003824	molecular_function	catalytic activity
E	0004165	molecular_function	delta(3)-delta(2)-enoyl-CoA isomerase activity
E	0004300	molecular_function	enoyl-CoA hydratase activity
E	0005515	molecular_function	protein binding
E	0005739	cellular_component	mitochondrion
E	0005759	cellular_component	mitochondrial matrix
E	0006629	biological_process	lipid metabolic process
E	0006631	biological_process	fatty acid metabolic process
E	0006635	biological_process	fatty acid beta-oxidation
E	0009083	biological_process	branched-chain amino acid catabolic process
E	0016829	molecular_function	lyase activity
E	0016853	molecular_function	isomerase activity
E	0018812	molecular_function	3-hydroxyacyl-CoA dehydratase activity
E	0043956	molecular_function	3-hydroxypropionyl-CoA dehydratase activity
E	0120092	molecular_function	(2E)-butenoyl-CoA hydratase activity
F	0003824	molecular_function	catalytic activity
F	0004165	molecular_function	delta(3)-delta(2)-enoyl-CoA isomerase activity
F	0004300	molecular_function	enoyl-CoA hydratase activity
F	0005515	molecular_function	protein binding
F	0005739	cellular_component	mitochondrion
F	0005759	cellular_component	mitochondrial matrix
F	0006629	biological_process	lipid metabolic process
F	0006631	biological_process	fatty acid metabolic process
F	0006635	biological_process	fatty acid beta-oxidation
F	0009083	biological_process	branched-chain amino acid catabolic process
F	0016829	molecular_function	lyase activity
F	0016853	molecular_function	isomerase activity
F	0018812	molecular_function	3-hydroxyacyl-CoA dehydratase activity
F	0043956	molecular_function	3-hydroxypropionyl-CoA dehydratase activity
F	0120092	molecular_function	(2E)-butenoyl-CoA hydratase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE MG C 291

Chain	Residue
C	GLU164

site_id	AC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE MG D 291

Chain	Residue
D	GLU164

site_id	AC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE MG C 292

Chain	Residue
C	ALA206

site_id	AC4
Number of Residues	11
Details	BINDING SITE FOR RESIDUE COO B 1

Chain	Residue
D	LYS92
D	ALA98
D	ASP99
D	ILE100
D	LYS101
A	PHE279
A	LYS282
C	COO2
D	LYS56
D	ALA57
D	ALA60

site_id	AC5
Number of Residues	13
Details	BINDING SITE FOR RESIDUE COO C 2

Chain	Residue
A	LYS282
B	COO1
B	PHE279
C	LYS56
C	ALA57
C	ALA60
C	LYS92
C	ALA98
C	ASP99
C	ILE100
C	LYS101
C	TYR137
C	PHE139

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ILE131-ILE151

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	6
Details	Site: {"description":"Important for catalytic activity","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	6
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	12
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q8BH95","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	6
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	6
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	6
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q8BH95","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	6
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q8BH95","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1dub

Chain	Residue	Details
A	ALA98
A	GLU164
A	GLY141
A	GLU144

site_id	CSA10
Number of Residues	2
Details	Annotated By Reference To The Literature 1dub

Chain	Residue	Details
D	GLY172
D	GLU164

site_id	CSA11
Number of Residues	2
Details	Annotated By Reference To The Literature 1dub

Chain	Residue	Details
E	GLY172
E	GLU164

site_id	CSA12
Number of Residues	2
Details	Annotated By Reference To The Literature 1dub

Chain	Residue	Details
F	GLY172
F	GLU164

site_id	CSA13
Number of Residues	3
Details	Annotated By Reference To The Literature 1dub

Chain	Residue	Details
A	GLU164
A	GLY141
A	GLU144

site_id	CSA14
Number of Residues	3
Details	Annotated By Reference To The Literature 1dub

Chain	Residue	Details
B	GLU164
B	GLY141
B	GLU144

site_id	CSA15
Number of Residues	3
Details	Annotated By Reference To The Literature 1dub

Chain	Residue	Details
C	GLU164
C	GLY141
C	GLU144

site_id	CSA16
Number of Residues	3
Details	Annotated By Reference To The Literature 1dub

Chain	Residue	Details
D	GLU164
D	GLY141
D	GLU144

site_id	CSA17
Number of Residues	3
Details	Annotated By Reference To The Literature 1dub

Chain	Residue	Details
E	GLU164
E	GLY141
E	GLU144

site_id	CSA18
Number of Residues	3
Details	Annotated By Reference To The Literature 1dub

Chain	Residue	Details
F	GLU164
F	GLY141
F	GLU144

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1dub

Chain	Residue	Details
B	ALA98
B	GLU164
B	GLY141
B	GLU144

site_id	CSA3
Number of Residues	4
Details	Annotated By Reference To The Literature 1dub

Chain	Residue	Details
C	ALA98
C	GLU164
C	GLY141
C	GLU144

site_id	CSA4
Number of Residues	4
Details	Annotated By Reference To The Literature 1dub

Chain	Residue	Details
D	ALA98
D	GLU164
D	GLY141
D	GLU144

site_id	CSA5
Number of Residues	4
Details	Annotated By Reference To The Literature 1dub

Chain	Residue	Details
E	ALA98
E	GLU164
E	GLY141
E	GLU144

site_id	CSA6
Number of Residues	4
Details	Annotated By Reference To The Literature 1dub

Chain	Residue	Details
F	ALA98
F	GLU164
F	GLY141
F	GLU144

site_id	CSA7
Number of Residues	2
Details	Annotated By Reference To The Literature 1dub

Chain	Residue	Details
A	GLY172
A	GLU164

site_id	CSA8
Number of Residues	2
Details	Annotated By Reference To The Literature 1dub

Chain	Residue	Details
B	GLY172
B	GLU164

site_id	CSA9
Number of Residues	2
Details	Annotated By Reference To The Literature 1dub

Chain	Residue	Details
C	GLY172
C	GLU164

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)