3N6R

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

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004658	molecular_function	propionyl-CoA carboxylase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0016042	biological_process	lipid catabolic process
A	0016874	molecular_function	ligase activity
A	0046872	molecular_function	metal ion binding
B	0004658	molecular_function	propionyl-CoA carboxylase activity
B	0005515	molecular_function	protein binding
B	0016874	molecular_function	ligase activity
C	0004658	molecular_function	propionyl-CoA carboxylase activity
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0016042	biological_process	lipid catabolic process
C	0016874	molecular_function	ligase activity
C	0046872	molecular_function	metal ion binding
D	0004658	molecular_function	propionyl-CoA carboxylase activity
D	0005515	molecular_function	protein binding
D	0016874	molecular_function	ligase activity
E	0004658	molecular_function	propionyl-CoA carboxylase activity
E	0005515	molecular_function	protein binding
E	0005524	molecular_function	ATP binding
E	0016042	biological_process	lipid catabolic process
E	0016874	molecular_function	ligase activity
E	0046872	molecular_function	metal ion binding
F	0004658	molecular_function	propionyl-CoA carboxylase activity
F	0005515	molecular_function	protein binding
F	0016874	molecular_function	ligase activity
G	0004658	molecular_function	propionyl-CoA carboxylase activity
G	0005515	molecular_function	protein binding
G	0005524	molecular_function	ATP binding
G	0016042	biological_process	lipid catabolic process
G	0016874	molecular_function	ligase activity
G	0046872	molecular_function	metal ion binding
H	0004658	molecular_function	propionyl-CoA carboxylase activity
H	0005515	molecular_function	protein binding
H	0016874	molecular_function	ligase activity
I	0004658	molecular_function	propionyl-CoA carboxylase activity
I	0005515	molecular_function	protein binding
I	0005524	molecular_function	ATP binding
I	0016042	biological_process	lipid catabolic process
I	0016874	molecular_function	ligase activity
I	0046872	molecular_function	metal ion binding
J	0004658	molecular_function	propionyl-CoA carboxylase activity
J	0005515	molecular_function	protein binding
J	0016874	molecular_function	ligase activity
K	0004658	molecular_function	propionyl-CoA carboxylase activity
K	0005515	molecular_function	protein binding
K	0005524	molecular_function	ATP binding
K	0016042	biological_process	lipid catabolic process
K	0016874	molecular_function	ligase activity
K	0046872	molecular_function	metal ion binding
L	0004658	molecular_function	propionyl-CoA carboxylase activity
L	0005515	molecular_function	protein binding
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	6
Details	ACT_SITE: ACT_SITE => ECO:0000250

Chain	Residue	Details
A	GLU349
C	GLU349
E	GLU349
G	GLU349
I	GLU349
K	GLU349

---

site_id	SWS_FT_FI2
Number of Residues	18
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	LYS177
G	LYS177
G	GLU261
G	ASN296
I	LYS177
I	GLU261
I	ASN296
K	LYS177
K	GLU261
K	ASN296
A	GLU261
A	ASN296
C	LYS177
C	GLU261
C	ASN296
E	LYS177
E	GLU261
E	ASN296

---

site_id	SWS_FT_FI3
Number of Residues	6
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00409

Chain	Residue	Details
A	SER209
C	SER209
E	SER209
G	SER209
I	SER209
K	SER209

---

site_id	SWS_FT_FI4
Number of Residues	18
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00409, ECO:0000255|PROSITE-ProRule:PRU00969

Chain	Residue	Details
A	GLU336
G	GLU336
G	GLU349
G	ASN351
I	GLU336
I	GLU349
I	ASN351
K	GLU336
K	GLU349
K	ASN351
A	GLU349
A	ASN351
C	GLU336
C	GLU349
C	ASN351
E	GLU336
E	GLU349
E	ASN351

---

site_id	SWS_FT_FI5
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:20725044, ECO:0007744|PDB:3N6R

Chain	Residue	Details
A	PHE409
C	PHE409
E	PHE409
G	PHE409
I	PHE409
K	PHE409

---

site_id	SWS_FT_FI6
Number of Residues	6
Details	MOD_RES: N6-biotinyllysine => ECO:0000255|PROSITE-ProRule:PRU01066, ECO:0000269|PubMed:20725044, ECO:0007744|PDB:3N6R

Chain	Residue	Details
A	LYS694
C	LYS694
E	LYS694
G	LYS694
I	LYS694
K	LYS694

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