Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5LP7

Crystal structure of 3-Ketoacyl-CoA Thiolase (MmgA) from Bacillus subtilis.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003985	molecular_function	acetyl-CoA C-acetyltransferase activity
A	0003988	molecular_function	acetyl-CoA C-acyltransferase activity
A	0005737	cellular_component	cytoplasm
A	0016740	molecular_function	transferase activity
A	0016746	molecular_function	acyltransferase activity
A	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
A	0030435	biological_process	sporulation resulting in formation of a cellular spore
B	0003985	molecular_function	acetyl-CoA C-acetyltransferase activity
B	0003988	molecular_function	acetyl-CoA C-acyltransferase activity
B	0005737	cellular_component	cytoplasm
B	0016740	molecular_function	transferase activity
B	0016746	molecular_function	acyltransferase activity
B	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
B	0030435	biological_process	sporulation resulting in formation of a cellular spore
C	0003985	molecular_function	acetyl-CoA C-acetyltransferase activity
C	0003988	molecular_function	acetyl-CoA C-acyltransferase activity
C	0005737	cellular_component	cytoplasm
C	0016740	molecular_function	transferase activity
C	0016746	molecular_function	acyltransferase activity
C	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
C	0030435	biological_process	sporulation resulting in formation of a cellular spore
D	0003985	molecular_function	acetyl-CoA C-acetyltransferase activity
D	0003988	molecular_function	acetyl-CoA C-acyltransferase activity
D	0005737	cellular_component	cytoplasm
D	0016740	molecular_function	transferase activity
D	0016746	molecular_function	acyltransferase activity
D	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
D	0030435	biological_process	sporulation resulting in formation of a cellular spore
E	0003985	molecular_function	acetyl-CoA C-acetyltransferase activity
E	0003988	molecular_function	acetyl-CoA C-acyltransferase activity
E	0005737	cellular_component	cytoplasm
E	0016740	molecular_function	transferase activity
E	0016746	molecular_function	acyltransferase activity
E	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
E	0030435	biological_process	sporulation resulting in formation of a cellular spore
F	0003985	molecular_function	acetyl-CoA C-acetyltransferase activity
F	0003988	molecular_function	acetyl-CoA C-acyltransferase activity
F	0005737	cellular_component	cytoplasm
F	0016740	molecular_function	transferase activity
F	0016746	molecular_function	acyltransferase activity
F	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
F	0030435	biological_process	sporulation resulting in formation of a cellular spore
G	0003985	molecular_function	acetyl-CoA C-acetyltransferase activity
G	0003988	molecular_function	acetyl-CoA C-acyltransferase activity
G	0005737	cellular_component	cytoplasm
G	0016740	molecular_function	transferase activity
G	0016746	molecular_function	acyltransferase activity
G	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
G	0030435	biological_process	sporulation resulting in formation of a cellular spore
H	0003985	molecular_function	acetyl-CoA C-acetyltransferase activity
H	0003988	molecular_function	acetyl-CoA C-acyltransferase activity
H	0005737	cellular_component	cytoplasm
H	0016740	molecular_function	transferase activity
H	0016746	molecular_function	acyltransferase activity
H	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
H	0030435	biological_process	sporulation resulting in formation of a cellular spore

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	binding site for residue GOL E 401

Chain	Residue
E	PHE17
E	GLY249
E	VAL250

site_id	AC2
Number of Residues	8
Details	binding site for residue GOL A 401

Chain	Residue
A	HOH513
A	HOH558
A	MET157
A	PRO248
A	GLY249
A	ALA319
A	PHE320
A	HIS349

site_id	AC3
Number of Residues	8
Details	binding site for residue GOL B 401

Chain	Residue
B	LYS25
B	ALA59
B	GLY60
B	SER61
B	ASN120
B	PRO122
B	HOH522
B	HOH594

site_id	AC4
Number of Residues	3
Details	binding site for residue GOL B 402

Chain	Residue
B	GLN100
B	PHE279
B	HOH512

site_id	AC5
Number of Residues	6
Details	binding site for residue GOL C 401

Chain	Residue
C	ARG93
C	GLN100
C	THR281
C	HOH526
C	HOH529
D	GLU49

site_id	AC6
Number of Residues	9
Details	binding site for residue GOL F 401

Chain	Residue
E	ARG93
E	GLN100
E	HOH573
F	GLU49
F	GLY50
F	PRO80
F	MET101
F	ASP106
F	HOH526

site_id	AC7
Number of Residues	7
Details	binding site for residue GOL G 401

Chain	Residue
G	LEU148
G	PRO248
G	GLY249
G	ALA319
G	PHE320
G	HIS349
G	HOH519

site_id	AC8
Number of Residues	6
Details	binding site for residue GOL D 401

Chain	Residue
C	MET101
D	ARG93
D	GLN100
D	PHE279
D	THR281
D	HOH518

site_id	AC9
Number of Residues	6
Details	binding site for Di-peptide ARG E 222 and ASP E 223

Chain	Residue
E	ALA187
E	ILE220
E	ARG221
E	THR224
E	GLN228
E	HOH518

Functional Information from PROSITE/UniProt

site_id	PS00098
Number of Residues	19
Details	THIOLASE_1 Thiolases acyl-enzyme intermediate signature. LNKvCASGLrAVtlcdqmI

Chain	Residue	Details
H	LEU84-ILE102

site_id	PS00099
Number of Residues	14
Details	THIOLASE_3 Thiolases active site. GVAAICSGaAqGdA

Chain	Residue	Details
H	GLY374-ALA387

site_id	PS00737
Number of Residues	17
Details	THIOLASE_2 Thiolases signature 2. NvnGGaIAlGHPiGaSG

Chain	Residue	Details
H	ASN339-GLY355

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Active site: {"description":"Acyl-thioester intermediate","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	16
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10020","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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