6ESQ

Structure of the acetoacetyl-CoA thiolase/HMG-CoA synthase complex from Methanothermococcus thermolithotrophicus soaked with acetyl-CoA

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003985	molecular_function	acetyl-CoA C-acetyltransferase activity
A	0016746	molecular_function	acyltransferase activity
A	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
B	0003985	molecular_function	acetyl-CoA C-acetyltransferase activity
B	0016746	molecular_function	acyltransferase activity
B	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
C	0003985	molecular_function	acetyl-CoA C-acetyltransferase activity
C	0016746	molecular_function	acyltransferase activity
C	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
D	0003985	molecular_function	acetyl-CoA C-acetyltransferase activity
D	0016746	molecular_function	acyltransferase activity
D	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
E	0046872	molecular_function	metal ion binding
F	0046872	molecular_function	metal ion binding
G	0046872	molecular_function	metal ion binding
H	0046872	molecular_function	metal ion binding
I	0016746	molecular_function	acyltransferase activity
J	0016746	molecular_function	acyltransferase activity
K	0016746	molecular_function	acyltransferase activity
L	0016746	molecular_function	acyltransferase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	binding site for residue COA A 401

Chain	Residue
A	PHE182
A	LEU203
A	CYS206
A	PRO208
A	LYS332
J	ARG203
J	LYS243

---

site_id	AC2
Number of Residues	7
Details	binding site for residue COA B 401

Chain	Residue
B	CYS206
B	SER207
B	PRO208
B	LYS332
L	ARG203
B	PHE182
B	LEU203

---

site_id	AC3
Number of Residues	3
Details	binding site for residue K B 402

Chain	Residue
B	ASP36
B	ASP356
D	GLU232

---

site_id	AC4
Number of Residues	2
Details	binding site for residue K B 403

Chain	Residue
B	ASP3
B	ARG392

---

site_id	AC5
Number of Residues	10
Details	binding site for residue COA C 401

Chain	Residue
C	PHE182
C	LEU203
C	MET204
C	CYS206
C	SER207
C	PRO208
C	VAL209
C	LYS332
I	ARG203
I	LYS243

---

site_id	AC6
Number of Residues	10
Details	binding site for residue COA D 401

Chain	Residue
D	THR122
D	PHE182
D	VAL197
D	LEU203
D	CYS206
D	SER207
D	PRO208
D	LYS332
K	ARG203
K	LYS243

---

site_id	AC7
Number of Residues	4
Details	binding site for residue ZN E 201

Chain	Residue
E	CYS20
E	CYS23
E	CYS34
E	CYS37

---

site_id	AC8
Number of Residues	3
Details	binding site for residue CL E 202

Chain	Residue
B	GLY41
E	ARG38
E	ARG39

---

site_id	AC9
Number of Residues	4
Details	binding site for residue ZN F 201

Chain	Residue
F	CYS20
F	CYS23
F	CYS34
F	CYS37

---

site_id	AD1
Number of Residues	3
Details	binding site for residue CL F 202

Chain	Residue
C	GLY41
F	ARG38
F	ARG39

---

site_id	AD2
Number of Residues	4
Details	binding site for residue ZN G 201

Chain	Residue
G	CYS20
G	CYS23
G	CYS34
G	CYS37

---

site_id	AD3
Number of Residues	3
Details	binding site for residue CL G 202

Chain	Residue
D	GLY41
G	ARG38
G	ARG39

---

site_id	AD4
Number of Residues	4
Details	binding site for residue ZN H 201

Chain	Residue
H	CYS20
H	CYS23
H	CYS34
H	CYS37

---

site_id	AD5
Number of Residues	2
Details	binding site for residue K I 401

Chain	Residue
I	GLU111
K	GLU111

---

site_id	AD6
Number of Residues	4
Details	binding site for residue NA K 401

Chain	Residue
I	VAL88
K	GLU111
K	PHE112
K	ALA113

---

site_id	AD7
Number of Residues	2
Details	binding site for residue K L 401

Chain	Residue
J	GLU111
L	GLU111

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