Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3HO8

Crystal Structure of S. aureus Pyruvate Carboxylase in complex with Coenzyme A

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
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	0000166	molecular_function	nucleotide 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	0000166	molecular_function	nucleotide 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	0000166	molecular_function	nucleotide 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	19
Details	BINDING SITE FOR RESIDUE COA A 2001

Chain	Residue
A	ARG398
A	LYS1056
A	ARG1057
A	MET1080
A	ASN1081
A	ARG1085
C	ARG77
C	TYR78
C	ALA80
C	ASP81
C	SER83
A	ARG448
A	GLU449
A	ARG451
A	ARG453
A	SER493
A	LEU494
A	ARG496
A	GLY1055

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

Chain	Residue
A	ASP572
A	LYS741
A	HIS771
A	HIS773

site_id	AC3
Number of Residues	19
Details	BINDING SITE FOR RESIDUE COA D 2001

Chain	Residue
B	ARG77
B	TYR78
B	LYS79
B	ALA80
B	ASP81
B	SER83
D	ARG398
D	ARG448
D	GLU449
D	ARG451
D	ARG453
D	SER493
D	LEU494
D	ARG496
D	GLY497
D	GLY1055
D	LYS1056
D	LEU1058
D	MET1080

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN D 2002

Chain	Residue
D	ARG571
D	ASP572
D	LYS741
D	HIS771
D	HIS773

site_id	AC5
Number of Residues	16
Details	BINDING SITE FOR RESIDUE COA C 2001

Chain	Residue
A	ARG77
A	TYR78
A	ALA80
A	ASP81
A	SER83
C	ARG398
C	ARG451
C	ARG453
C	SER493
C	LEU494
C	ARG496
C	ILE1052
C	LYS1056
C	ARG1057
C	ASN1081
C	ARG1085

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN C 2002

Chain	Residue
C	ASP572
C	LYS741
C	HIS771
C	HIS773

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE BTI C 2000

Chain	Residue
C	ASN506
C	GLY511
C	PHE512
C	PRO513
C	ASN617
C	PHE618
C	LYS620

site_id	AC8
Number of Residues	20
Details	BINDING SITE FOR RESIDUE COA B 2001

Chain	Residue
B	ARG398
B	GLU449
B	ARG451
B	ARG453
B	SER493
B	LEU494
B	ASP495
B	ARG496
B	GLY497
B	GLY1055
B	LYS1056
B	ARG1057
B	LEU1058
B	ASN1081
B	ARG1085
D	ARG77
D	TYR78
D	ALA80
D	ASP81
D	SER83

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MN B 2002

Chain	Residue
B	ASP572
B	HIS771
B	HIS773

site_id	BC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE BTI B 2000

Chain	Residue
B	GLY511
B	PHE512
B	PRO513
B	PHE618
B	LYS620
B	PHE1038
B	TYR503
B	ASN506

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	1076
Details	Domain: {"description":"Pyruvate carboxyltransferase","evidences":[{"source":"PROSITE-ProRule","id":"PRU01151","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"evidences":[{"source":"UniProtKB","id":"Q9KWU4","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"19523900","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23286247","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3BG5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4HNT","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"19523900","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23286247","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3BG5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4HNT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4HNV","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PubMed","id":"19523900","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3BG5","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"19523900","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23286247","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3HB9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3HBL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4HNT","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"19523900","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23286247","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3HB9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3HBL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4HNV","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	4
Details	Modified residue: {"description":"N6-carboxylysine","evidences":[{"source":"UniProtKB","id":"P11498","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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