3BG9

Crystal Structure of Human Pyruvate Carboxylase (missing the biotin carboxylase domain at the N-terminus) F1077A Mutant

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004736	molecular_function	pyruvate carboxylase activity
A	0005524	molecular_function	ATP binding
A	0006090	biological_process	pyruvate metabolic process
A	0006094	biological_process	gluconeogenesis
B	0003824	molecular_function	catalytic activity
B	0004736	molecular_function	pyruvate carboxylase activity
B	0005524	molecular_function	ATP binding
B	0006090	biological_process	pyruvate metabolic process
B	0006094	biological_process	gluconeogenesis
C	0003824	molecular_function	catalytic activity
C	0004736	molecular_function	pyruvate carboxylase activity
C	0005524	molecular_function	ATP binding
C	0006090	biological_process	pyruvate metabolic process
C	0006094	biological_process	gluconeogenesis
D	0003824	molecular_function	catalytic activity
D	0004736	molecular_function	pyruvate carboxylase activity
D	0005524	molecular_function	ATP binding
D	0006090	biological_process	pyruvate metabolic process
D	0006094	biological_process	gluconeogenesis

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN A 2001

Chain	Residue
A	ASP572
A	LYS741
A	HIS771
A	HIS773

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN B 2001

Chain	Residue
B	ASP572
B	LYS741
B	HIS771
B	HIS773

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN C 2001

Chain	Residue
C	LYS741
C	HIS771
C	HIS773
C	ASP572

---

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN D 2001

Chain	Residue
D	ASP572
D	LYS741
D	HIS771
D	HIS773

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	GLY1134-SER1151

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	BINDING:

Chain	Residue	Details
A	ARG571
D	ARG571
D	ARG644
D	THR908
A	ARG644
A	THR908
B	ARG571
B	ARG644
B	THR908
C	ARG571
C	ARG644
C	THR908

---

site_id	SWS_FT_FI2
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269|PubMed:18297087

Chain	Residue	Details
A	ASP572
D	ASP572
D	HIS771
D	HIS773
A	HIS771
A	HIS773
B	ASP572
B	HIS771
B	HIS773
C	ASP572
C	HIS771
C	HIS773

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: via carbamate group => ECO:0000269|PubMed:18297087

Chain	Residue	Details
A	LYS741
B	LYS741
C	LYS741
D	LYS741

---

site_id	SWS_FT_FI4
Number of Residues	36
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q05920

Chain	Residue	Details
A	LYS589
B	LYS589
B	LYS661
B	LYS717
B	LYS748
B	LYS892
B	LYS969
B	LYS992
B	LYS1061
B	LYS1124
C	LYS589
A	LYS661
C	LYS661
C	LYS717
C	LYS748
C	LYS892
C	LYS969
C	LYS992
C	LYS1061
C	LYS1124
D	LYS589
D	LYS661
A	LYS717
D	LYS717
D	LYS748
D	LYS892
D	LYS969
D	LYS992
D	LYS1061
D	LYS1124
A	LYS748
A	LYS892
A	LYS969
A	LYS992
A	LYS1061
A	LYS1124

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	MOD_RES: N6-carboxylysine => ECO:0000269|PubMed:18297087

Chain	Residue	Details
A	LYS741
B	LYS741
C	LYS741
D	LYS741

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P52873

Chain	Residue	Details
A	THR1003
B	THR1003
C	THR1003
D	THR1003

---

site_id	SWS_FT_FI7
Number of Residues	4
Details	MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861

Chain	Residue	Details
A	LYS1090
B	LYS1090
C	LYS1090
D	LYS1090

---

site_id	SWS_FT_FI8
Number of Residues	4
Details	MOD_RES: N6-biotinyllysine => ECO:0000255|PROSITE-ProRule:PRU01066, ECO:0000269|PubMed:6548474, ECO:0000269|PubMed:7918683

Chain	Residue	Details
A	LYS1144
B	LYS1144
C	LYS1144
D	LYS1144

---