Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3N6R

CRYSTAL STRUCTURE OF the holoenzyme of PROPIONYL-COA CARBOXYLASE (PCC)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0004658	molecular_function	propionyl-CoA carboxylase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0006629	biological_process	lipid metabolic process
A	0016042	biological_process	lipid catabolic process
A	0016874	molecular_function	ligase activity
A	0046872	molecular_function	metal ion binding
B	0003989	molecular_function	acetyl-CoA carboxylase activity
B	0004658	molecular_function	propionyl-CoA carboxylase activity
B	0005515	molecular_function	protein binding
B	0009317	cellular_component	acetyl-CoA carboxylase complex
B	0015977	biological_process	carbon fixation
B	0016874	molecular_function	ligase activity
C	0000166	molecular_function	nucleotide binding
C	0004658	molecular_function	propionyl-CoA carboxylase activity
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0006629	biological_process	lipid metabolic process
C	0016042	biological_process	lipid catabolic process
C	0016874	molecular_function	ligase activity
C	0046872	molecular_function	metal ion binding
D	0003989	molecular_function	acetyl-CoA carboxylase activity
D	0004658	molecular_function	propionyl-CoA carboxylase activity
D	0005515	molecular_function	protein binding
D	0009317	cellular_component	acetyl-CoA carboxylase complex
D	0015977	biological_process	carbon fixation
D	0016874	molecular_function	ligase activity
E	0000166	molecular_function	nucleotide binding
E	0004658	molecular_function	propionyl-CoA carboxylase activity
E	0005515	molecular_function	protein binding
E	0005524	molecular_function	ATP binding
E	0006629	biological_process	lipid metabolic process
E	0016042	biological_process	lipid catabolic process
E	0016874	molecular_function	ligase activity
E	0046872	molecular_function	metal ion binding
F	0003989	molecular_function	acetyl-CoA carboxylase activity
F	0004658	molecular_function	propionyl-CoA carboxylase activity
F	0005515	molecular_function	protein binding
F	0009317	cellular_component	acetyl-CoA carboxylase complex
F	0015977	biological_process	carbon fixation
F	0016874	molecular_function	ligase activity
G	0000166	molecular_function	nucleotide binding
G	0004658	molecular_function	propionyl-CoA carboxylase activity
G	0005515	molecular_function	protein binding
G	0005524	molecular_function	ATP binding
G	0006629	biological_process	lipid metabolic process
G	0016042	biological_process	lipid catabolic process
G	0016874	molecular_function	ligase activity
G	0046872	molecular_function	metal ion binding
H	0003989	molecular_function	acetyl-CoA carboxylase activity
H	0004658	molecular_function	propionyl-CoA carboxylase activity
H	0005515	molecular_function	protein binding
H	0009317	cellular_component	acetyl-CoA carboxylase complex
H	0015977	biological_process	carbon fixation
H	0016874	molecular_function	ligase activity
I	0000166	molecular_function	nucleotide binding
I	0004658	molecular_function	propionyl-CoA carboxylase activity
I	0005515	molecular_function	protein binding
I	0005524	molecular_function	ATP binding
I	0006629	biological_process	lipid metabolic process
I	0016042	biological_process	lipid catabolic process
I	0016874	molecular_function	ligase activity
I	0046872	molecular_function	metal ion binding
J	0003989	molecular_function	acetyl-CoA carboxylase activity
J	0004658	molecular_function	propionyl-CoA carboxylase activity
J	0005515	molecular_function	protein binding
J	0009317	cellular_component	acetyl-CoA carboxylase complex
J	0015977	biological_process	carbon fixation
J	0016874	molecular_function	ligase activity
K	0000166	molecular_function	nucleotide binding
K	0004658	molecular_function	propionyl-CoA carboxylase activity
K	0005515	molecular_function	protein binding
K	0005524	molecular_function	ATP binding
K	0006629	biological_process	lipid metabolic process
K	0016042	biological_process	lipid catabolic process
K	0016874	molecular_function	ligase activity
K	0046872	molecular_function	metal ion binding
L	0003989	molecular_function	acetyl-CoA carboxylase activity
L	0004658	molecular_function	propionyl-CoA carboxylase activity
L	0005515	molecular_function	protein binding
L	0009317	cellular_component	acetyl-CoA carboxylase complex
L	0015977	biological_process	carbon fixation
L	0016874	molecular_function	ligase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE BTI A 801

Chain	Residue
A	MET693
A	LYS694
B	PHE397
B	PRO399
J	VAL234

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE BTI C 801

Chain	Residue
L	THR226
L	VAL234
C	LYS694
D	CYS365
D	GLY396
D	PHE397

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE BTI E 801

Chain	Residue
E	MET693
E	LYS694
F	CYS365
F	PHE397
F	PRO399
H	THR226

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE BTI G 801

Chain	Residue
F	VAL234
G	LYS694
H	CYS365
H	GLY396
H	PHE397

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE BTI I 801

Chain	Residue
B	VAL234
I	MET693
I	LYS694
J	CYS365
J	GLY396
J	PHE397
J	PRO399

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE BTI K 801

Chain	Residue
D	VAL234
K	MET693
K	LYS694
L	CYS365
L	GLY396
L	PHE397

Functional Information from PROSITE/UniProt

site_id	PS00188
Number of Residues	18
Details	BIOTIN Biotin-requiring enzymes attachment site. GQaLctIeAMKMeniLrA

Chain	Residue	Details
A	GLY684-ALA701

site_id	PS00866
Number of Residues	15
Details	CPSASE_1 Carbamoyl-phosphate synthase subdomain signature 1. YPVMIKASaggGGkG

Chain	Residue	Details
A	TYR214-GLY228

site_id	PS00867
Number of Residues	8
Details	CPSASE_2 Carbamoyl-phosphate synthase subdomain signature 2. FLEMNTRL

Chain	Residue	Details
A	PHE347-LEU354

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	474
Details	Domain: {"description":"Biotinyl-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU01066","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	6
Details	Active site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	15
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	18
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00409","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU00969","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"20725044","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3N6R","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	6
Details	Modified residue: {"description":"N6-biotinyllysine","evidences":[{"source":"PROSITE-ProRule","id":"PRU01066","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"20725044","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3N6R","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	1458
Details	Domain: {"description":"CoA carboxyltransferase C-terminal","evidences":[{"source":"PROSITE-ProRule","id":"PRU01137","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	198
Details	Region: {"description":"Acyl-CoA binding","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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