4IEN

Crystal Structure of Acyl-CoA Hydrolase from Neisseria meningitidis FAM18

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006637	biological_process	acyl-CoA metabolic process
A	0016787	molecular_function	hydrolase activity
A	0016790	molecular_function	thiolester hydrolase activity
A	0052816	molecular_function	long-chain fatty acyl-CoA hydrolase activity
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006637	biological_process	acyl-CoA metabolic process
B	0016787	molecular_function	hydrolase activity
B	0016790	molecular_function	thiolester hydrolase activity
B	0052816	molecular_function	long-chain fatty acyl-CoA hydrolase activity
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006637	biological_process	acyl-CoA metabolic process
C	0016787	molecular_function	hydrolase activity
C	0016790	molecular_function	thiolester hydrolase activity
C	0052816	molecular_function	long-chain fatty acyl-CoA hydrolase activity
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006637	biological_process	acyl-CoA metabolic process
D	0016787	molecular_function	hydrolase activity
D	0016790	molecular_function	thiolester hydrolase activity
D	0052816	molecular_function	long-chain fatty acyl-CoA hydrolase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	19
Details	BINDING SITE FOR RESIDUE COA A 201

Chain	Residue
A	THR56
A	HOH305
A	HOH328
A	HOH341
A	HOH359
B	VAL29
B	LEU34
B	PHE64
B	LYS65
B	GLU66
B	PRO67
A	LEU57
A	GLY84
A	ARG85
A	THR86
A	SER87
A	ARG146
A	SER149
A	HOH302

---

site_id	AC2
Number of Residues	18
Details	BINDING SITE FOR RESIDUE GDP A 202

Chain	Residue
A	GLU11
A	TYR77
A	ALA78
A	ALA79
A	ASN81
A	GLY91
A	ILE92
A	ARG93
A	HIS106
A	SER109
A	TYR111
A	ARG138
A	LYS141
B	ARG5
B	ASP155
B	MET156
B	SER157
B	CYS158

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL A 203

Chain	Residue
A	ASN24
A	GLY31
B	THR56
B	HOH354

---

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL B 201

Chain	Residue
A	THR56
A	HOH377
B	ASN24
B	GLY31

---

site_id	AC5
Number of Residues	19
Details	BINDING SITE FOR RESIDUE COA B 202

Chain	Residue
A	VAL29
A	LEU34
A	PHE64
A	LYS65
A	GLU66
A	PRO67
B	THR56
B	LEU57
B	GLY84
B	ARG85
B	THR86
B	SER87
B	PRO122
B	ARG146
B	SER149
B	HOH303
B	HOH305
B	HOH347
C	GLU129

---

site_id	AC6
Number of Residues	19
Details	BINDING SITE FOR RESIDUE GDP B 203

Chain	Residue
A	ARG5
A	ASP155
A	MET156
A	SER157
A	CYS158
B	GLU11
B	TYR77
B	ALA78
B	ALA79
B	ASN81
B	GLY91
B	ILE92
B	ARG93
B	HIS106
B	SER109
B	TYR111
B	ARG138
B	LYS141
B	HOH342

---

site_id	AC7
Number of Residues	18
Details	BINDING SITE FOR RESIDUE COA C 201

Chain	Residue
D	GLU66
D	PRO67
C	THR56
C	LEU57
C	GLY84
C	ARG85
C	THR86
C	SER87
C	PRO122
C	ARG146
C	SER149
C	HOH302
C	HOH307
C	HOH370
D	VAL29
D	LEU34
D	PHE64
D	LYS65

---

site_id	AC8
Number of Residues	19
Details	BINDING SITE FOR RESIDUE GDP C 202

Chain	Residue
C	GLU11
C	TYR77
C	ALA78
C	ALA79
C	ASN81
C	GLY91
C	ILE92
C	ARG93
C	HIS106
C	SER109
C	TYR111
C	ARG138
C	LYS141
C	HOH336
C	HOH366
D	ARG5
D	ASP155
D	SER157
D	CYS158

---

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL C 203

Chain	Residue
C	ASN24
C	GLY31
C	HOH303
D	THR56
D	HOH360

---

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL D 201

Chain	Residue
C	THR56
C	HOH362
D	ASN24
D	GLY31

---

site_id	BC2
Number of Residues	22
Details	BINDING SITE FOR RESIDUE COA D 202

Chain	Residue
C	VAL29
C	LEU34
C	PHE64
C	LYS65
C	GLU66
C	PRO67
D	THR56
D	LEU57
D	GLY84
D	ARG85
D	THR86
D	SER87
D	PRO122
D	ARG146
D	SER149
D	HOH304
D	HOH306
D	HOH323
D	HOH332
D	HOH343
D	HOH354
D	HOH366

---

site_id	BC3
Number of Residues	17
Details	BINDING SITE FOR RESIDUE GDP D 203

Chain	Residue
C	ARG5
C	ASP155
C	MET156
C	SER157
C	CYS158
D	GLU11
D	TYR77
D	ALA78
D	ALA79
D	ASN81
D	GLY91
D	ILE92
D	ARG93
D	SER109
D	TYR111
D	ARG138
D	HOH341

---