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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4ZDB

Yeast enoyl-CoA isomerase (ScECI2) complexed with acetoacetyl-CoA

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue SO4 A 301

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

site_id	AC2
Number of Residues	5
Details	binding site for residue SO4 A 302

Chain	Residue
C	PRO227
A	LYS257
A	TYR258
A	HOH502
C	TYR225

site_id	AC3
Number of Residues	7
Details	binding site for residue SO4 A 303

Chain	Residue
A	SER62
A	GLY63
A	ALA206
A	GLU207
A	SO4304
A	HOH404
A	HOH416

site_id	AC4
Number of Residues	2
Details	binding site for residue SO4 A 304

Chain	Residue
A	PRO27
A	SO4303

site_id	AC5
Number of Residues	15
Details	binding site for residue CAA A 305

Chain	Residue
A	ASP28
A	ASN29
A	LEU30
A	ALA32
A	PHE65
A	SER68
A	ALA70
A	ASP71
A	PHE72
A	LYS73
A	ILE124
A	PRO149
A	ASN152
A	ASN181
A	HOH408

site_id	AC6
Number of Residues	6
Details	binding site for residue GOL A 306

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

site_id	AC7
Number of Residues	10
Details	binding site for residue GOL A 307

Chain	Residue
A	ILE109
A	LEU133
A	LYS233
A	LYS237
A	PHE244
A	HOH415
A	HOH433
A	HOH483
B	TYR175
B	HOH412

site_id	AC8
Number of Residues	3
Details	binding site for residue GOL A 308

Chain	Residue
A	GLU9
A	ILE25
A	ASN26

site_id	AC9
Number of Residues	5
Details	binding site for residue SO4 B 301

Chain	Residue
B	ARG64
B	LYS143
B	PRO202
B	SER203
B	SER204

site_id	AD1
Number of Residues	5
Details	binding site for residue SO4 B 302

Chain	Residue
B	GLY63
B	SER204
B	ASN205
B	ALA206
B	GLU207

site_id	AD2
Number of Residues	14
Details	binding site for residue CAA B 303

Chain	Residue
B	ASP28
B	ASN29
B	LEU30
B	ALA32
B	PHE65
B	SER68
B	ALA70
B	ASP71
B	PHE72
B	LYS73
B	ILE124
B	LEU147
B	ASN181
B	HOH471

site_id	AD3
Number of Residues	6
Details	binding site for residue GOL B 304

Chain	Residue
B	GLY69
B	ALA70
B	GLY125
B	LEU126
B	LEU155
B	GLU158

site_id	AD4
Number of Residues	9
Details	binding site for residue GOL B 305

Chain	Residue
B	ILE109
B	LEU133
B	LYS233
B	LYS237
B	PHE244
B	HOH403
B	HOH416
B	HOH421
C	HOH412

site_id	AD5
Number of Residues	5
Details	binding site for residue SO4 C 301

Chain	Residue
C	ARG64
C	LYS143
C	PRO202
C	SER203
C	SER204

site_id	AD6
Number of Residues	6
Details	binding site for residue SO4 C 302

Chain	Residue
C	ALA206
C	GLU207
C	HOH401
C	HOH460
C	SER62
C	GLY63

site_id	AD7
Number of Residues	15
Details	binding site for residue CAA C 303

Chain	Residue
C	ASP28
C	ASN29
C	LEU30
C	ALA32
C	PHE65
C	SER68
C	ALA70
C	ASP71
C	PHE72
C	LYS73
C	LEU147
C	PRO149
C	ASN152
C	ASN181
C	HOH476

site_id	AD8
Number of Residues	6
Details	binding site for residue GOL C 304

Chain	Residue
C	ALA70
C	ARG100
C	GLY125
C	LEU126
C	LEU155
C	GLU158

site_id	AD9
Number of Residues	10
Details	binding site for residue GOL C 305

Chain	Residue
A	TYR175
A	HOH411
C	ILE109
C	LEU133
C	LYS233
C	LYS237
C	PHE244
C	HOH407
C	HOH423
C	HOH450

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	ACT_SITE: Proton donor/acceptor => ECO:0000269\|PubMed:26527136

Chain	Residue	Details
A	GLU158
B	GLU158
C	GLU158

site_id	SWS_FT_FI2
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269\|PubMed:26527136, ECO:0007744\|PDB:4ZDB, ECO:0007744\|PDB:4ZDC

Chain	Residue	Details
A	SER68
B	SER68
C	SER68

site_id	SWS_FT_FI3
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269\|PubMed:26527136, ECO:0007744\|PDB:4ZDC

Chain	Residue	Details
A	LEU126
B	LEU126
C	LEU126

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

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

site_id	MCSA3
Number of Residues	4
Details	M-CSA 499

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

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PDB entries from 2024-07-17

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