Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6OKC

Crosslinked Crystal Structure of Type II Fatty Acid Synthase Ketosynthase, FabB, and C12-crypto Acyl Carrier Protein, AcpP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004315	molecular_function	3-oxoacyl-[acyl-carrier-protein] synthase activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006633	biological_process	fatty acid biosynthetic process
A	0016746	molecular_function	acyltransferase activity
A	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
A	0044281	biological_process	small molecule metabolic process
A	1903966	biological_process	monounsaturated fatty acid biosynthetic process
B	0004315	molecular_function	3-oxoacyl-[acyl-carrier-protein] synthase activity
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006633	biological_process	fatty acid biosynthetic process
B	0016746	molecular_function	acyltransferase activity
B	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
B	0044281	biological_process	small molecule metabolic process
B	1903966	biological_process	monounsaturated fatty acid biosynthetic process
C	0000035	molecular_function	acyl binding
C	0000036	molecular_function	acyl carrier activity
C	0005515	molecular_function	protein binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006633	biological_process	fatty acid biosynthetic process
C	0008289	molecular_function	lipid binding
C	0008610	biological_process	lipid biosynthetic process
C	0009245	biological_process	lipid A biosynthetic process
C	0009410	biological_process	response to xenobiotic stimulus
C	0031177	molecular_function	phosphopantetheine binding
D	0000035	molecular_function	acyl binding
D	0000036	molecular_function	acyl carrier activity
D	0005515	molecular_function	protein binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006633	biological_process	fatty acid biosynthetic process
D	0008289	molecular_function	lipid binding
D	0008610	biological_process	lipid biosynthetic process
D	0009245	biological_process	lipid A biosynthetic process
D	0009410	biological_process	response to xenobiotic stimulus
D	0031177	molecular_function	phosphopantetheine binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	33
Details	binding site for Di-peptide MRJ A 501 and SER D 36

Chain	Residue
A	THR34
A	GLY107
A	ALA162
A	CYS163
A	MET197
A	GLU200
A	PHE201
A	VAL270
A	THR300
A	THR302
A	VAL304
A	PHE35
A	PHE390
A	GLY391
A	PHE392
A	HOH603
A	HOH620
A	HOH751
A	HOH784
B	GLN113
D	ASP35
D	LEU37
A	GLN37
D	ASP38
D	THR39
D	VAL40
D	HOH133
A	GLU38
A	LEU39
A	LYS40
A	HIS47
A	TRP49
A	GLY106

site_id	AC2
Number of Residues	33
Details	binding site for Di-peptide MRJ A 501 and SER D 36

Chain	Residue
A	THR34
A	PHE35
A	GLN37
A	GLU38
A	LEU39
A	LYS40
A	HIS47
A	TRP49
A	GLY106
A	GLY107
A	ALA162
A	CYS163
A	MET197
A	GLU200
A	PHE201
A	VAL270
A	THR300
A	THR302
A	VAL304
A	PHE390
A	GLY391
A	PHE392
A	HOH603
A	HOH620
A	HOH751
A	HOH784
B	GLN113
D	ASP35
D	LEU37
D	ASP38
D	THR39
D	VAL40
D	HOH133

site_id	AC3
Number of Residues	31
Details	binding site for Di-peptide MRJ B 501 and SER C 36

Chain	Residue
A	GLN113
A	MET138
B	THR34
B	PHE35
B	GLN37
B	GLU38
B	LEU39
B	LYS40
B	HIS47
B	TRP49
B	GLY106
B	ALA162
B	CYS163
B	MET197
B	GLU200
B	PHE201
B	VAL270
B	THR300
B	THR302
B	PHE390
B	GLY391
B	PHE392
B	HOH605
B	HOH621
B	HOH748
C	ASP35
C	LEU37
C	ASP38
C	THR39
C	VAL40
C	HOH212

Functional Information from PROSITE/UniProt

site_id	PS00012
Number of Residues	16
Details	PHOSPHOPANTETHEINE Phosphopantetheine attachment site. DLGADSLDTVELVMAL

Chain	Residue	Details
C	ASP31-LEU46

site_id	PS00606
Number of Residues	17
Details	KS3_1 Ketosynthase family 3 (KS3) active site signature. GVNysISsACATSahCI

Chain	Residue	Details
A	GLY154-ILE170

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	MOD_RES: O-(pantetheine 4'-phosphoryl)serine => ECO:0000255\|PROSITE-ProRule:PRU00258, ECO:0000269\|PubMed:4882207

Chain	Residue	Details
C	SER36
D	SER36

site_id	SWS_FT_FI2
Number of Residues	4
Details	ACT_SITE: For beta-ketoacyl synthase activity => ECO:0000255\|PROSITE-ProRule:PRU01348

Chain	Residue	Details
A	HIS298
A	HIS333
B	HIS298
B	HIS333

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	6
Details	M-CSA 292

Chain	Residue	Details
A	CYS163	activator, covalently attached, electrostatic stabiliser, hydrogen bond donor, nucleofuge, nucleophile
A	HIS298	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	LYS328	activator, hydrogen bond donor
A	HIS333	electrostatic stabiliser, hydrogen bond donor, increase basicity
A	PHE390	activator, hydrogen bond acceptor
A	PHE392	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA2
Number of Residues	6
Details	M-CSA 292

Chain	Residue	Details
B	CYS163	activator, covalently attached, electrostatic stabiliser, hydrogen bond donor, nucleofuge, nucleophile
B	HIS298	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	LYS328	activator, hydrogen bond donor
B	HIS333	electrostatic stabiliser, hydrogen bond donor, increase basicity
B	PHE390	activator, hydrogen bond acceptor
B	PHE392	electrostatic stabiliser, hydrogen bond donor

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