Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3HBL

Crystal Structure of S. aureus Pyruvate Carboxylase T908A 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	0005737	cellular_component	cytoplasm
A	0006090	biological_process	pyruvate metabolic process
A	0006094	biological_process	gluconeogenesis
A	0016874	molecular_function	ligase activity
A	0042802	molecular_function	identical protein binding
A	0046872	molecular_function	metal ion binding
B	0003824	molecular_function	catalytic activity
B	0004736	molecular_function	pyruvate carboxylase activity
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0006090	biological_process	pyruvate metabolic process
B	0006094	biological_process	gluconeogenesis
B	0016874	molecular_function	ligase activity
B	0042802	molecular_function	identical protein binding
B	0046872	molecular_function	metal ion binding
C	0003824	molecular_function	catalytic activity
C	0004736	molecular_function	pyruvate carboxylase activity
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0006090	biological_process	pyruvate metabolic process
C	0006094	biological_process	gluconeogenesis
C	0016874	molecular_function	ligase activity
C	0042802	molecular_function	identical protein binding
C	0046872	molecular_function	metal ion binding
D	0003824	molecular_function	catalytic activity
D	0004736	molecular_function	pyruvate carboxylase activity
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0006090	biological_process	pyruvate metabolic process
D	0006094	biological_process	gluconeogenesis
D	0016874	molecular_function	ligase activity
D	0042802	molecular_function	identical protein binding
D	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE BTI A 2000

Chain	Residue
A	LYS1144
B	ASN506
B	GLY511
B	PHE512
B	PHE618
B	LYS620

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN A 2002

Chain	Residue
A	HIS773
A	ASP572
A	LYS741
A	HIS771

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE BTI B 2000

Chain	Residue
A	TYR503
A	ASN506
A	GLY511
A	PHE512
A	PHE618
A	LYS620
B	LYS1144

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN B 2002

Chain	Residue
B	ASP572
B	LYS741
B	HIS771
B	HIS773

site_id	AC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE BTI C 2000

Chain	Residue
C	LYS1144
D	TYR503
D	ASN506
D	VAL507
D	GLY511
D	PHE512
D	PHE618
D	LYS620
D	PHE1038

site_id	AC6
Number of Residues	19
Details	BINDING SITE FOR RESIDUE ADP C 2100

Chain	Residue
C	LYS152
C	MET192
C	LYS194
C	GLY198
C	GLY199
C	GLY201
C	MET204
C	GLU236
C	ARG237
C	TYR238
C	ILE239
C	HIS244
C	GLN268
C	HIS271
C	GLU311
C	LEU313
C	ILE323
C	GLU324
C	THR478

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN C 2002

Chain	Residue
C	ASP572
C	LYS741
C	HIS771
C	HIS773

site_id	AC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE BTI D 2000

Chain	Residue
C	ASP613
C	PHE618
C	ARG644
C	TYR651
C	GLN870
C	ASN873
C	SER911
C	LYS912
D	LYS1144

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN D 2002

Chain	Residue
D	ASP572
D	LYS741
D	HIS771
D	HIS773

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	PHE189-GLY203

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

Chain	Residue	Details
A	PHE322-VAL329

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: ACT_SITE => ECO:0000250\|UniProtKB:Q9KWU4

Chain	Residue	Details
A	ARG328
B	ARG328
C	ARG328
D	ARG328

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:19523900, ECO:0000269\|PubMed:23286247, ECO:0007744\|PDB:3BG5, ECO:0007744\|PDB:4HNT

Chain	Residue	Details
A	LYS152
B	LYS152
C	LYS152
D	LYS152

site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269\|PubMed:19523900, ECO:0007744\|PDB:3BG5

Chain	Residue	Details
A	LYS194
A	ARG571
B	LYS194
B	ARG571
C	LYS194
C	ARG571
D	LYS194
D	ARG571

site_id	SWS_FT_FI4
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269\|PubMed:19523900, ECO:0000269\|PubMed:23286247, ECO:0007744\|PDB:3BG5, ECO:0007744\|PDB:4HNT, ECO:0007744\|PDB:4HNV

Chain	Residue	Details
A	HIS244
A	GLU311
B	HIS244
B	GLU311
C	HIS244
C	GLU311
D	HIS244
D	GLU311

site_id	SWS_FT_FI5
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:19523900, ECO:0000269\|PubMed:23286247, ECO:0007744\|PDB:3HB9, ECO:0007744\|PDB:3HBL, ECO:0007744\|PDB:4HNT

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_FI6
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:19523900, ECO:0000269\|PubMed:23286247, ECO:0007744\|PDB:3HB9, ECO:0007744\|PDB:3HBL, ECO:0007744\|PDB:4HNV

Chain	Residue	Details
A	LYS741
B	LYS741
C	LYS741
D	LYS741

site_id	SWS_FT_FI7
Number of Residues	4
Details	MOD_RES: N6-carboxylysine => ECO:0000250\|UniProtKB:P11498

Chain	Residue	Details
A	LYS741
B	LYS741
C	LYS741
D	LYS741

site_id	SWS_FT_FI8
Number of Residues	4
Details	MOD_RES: N6-biotinyllysine => ECO:0000255\|PROSITE-ProRule:PRU01066

Chain	Residue	Details
A	LYS1144
B	LYS1144
C	LYS1144
D	LYS1144

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