Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4HNV

Crystal structure of R54E mutant of S. aureus Pyruvate carboxylase

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	14
Details	BINDING SITE FOR RESIDUE ADP A 1201

Chain	Residue
A	LYS152
A	GLN268
A	HIS271
A	GLU311
A	LEU313
A	GLU324
A	ILE167
A	MET192
A	LYS194
A	GLU236
A	ARG237
A	TYR238
A	ILE239
A	HIS244

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN A 1202

Chain	Residue
A	ASP572
A	LYS741
A	HIS771
A	HIS773

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE BTI B 1201

Chain	Residue
A	LYS1144
B	ASN506
B	PHE512
B	PRO513
B	PHE618
B	LYS620

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE BTI B 1202

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

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN B 1203

Chain	Residue
B	ASP572
B	LYS741
B	HIS771
B	HIS773

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN C 1201

Chain	Residue
C	ASP572
C	LYS741
C	HIS771
C	HIS773

site_id	AC7
Number of Residues	22
Details	BINDING SITE FOR RESIDUE ATP C 1202

Chain	Residue
C	LYS152
C	MET192
C	LYS194
C	GLY198
C	GLY199
C	GLY200
C	GLY201
C	MET204
C	GLU236
C	ARG237
C	TYR238
C	ILE239
C	HIS244
C	GLN268
C	HIS271
C	LYS273
C	GLU311
C	LEU313
C	ILE323
C	GLU324
C	ASN326
C	THR478

site_id	AC8
Number of Residues	10
Details	BINDING SITE FOR RESIDUE BTI C 1203

Chain	Residue
C	GLN575
C	ASP613
C	ARG644
C	TYR651
C	GLY869
C	GLN870
C	THR908
C	SER911
C	LYS912
D	LYS1144

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL D 1201

Chain	Residue
A	LYS784
A	GLN785
D	LYS784
D	GLN785

site_id	BC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE BTI D 1202

Chain	Residue
C	LYS1144
D	ASN506
D	GLY511
D	PHE512
D	PRO513
D	PHE618
D	LYS620

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN D 1203

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	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	225
Details	Domain: {"description":"Biotinyl-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU01066","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Active site: {"evidences":[{"source":"UniProtKB","id":"Q9KWU4","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
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_FI5
Number of Residues	18
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	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_FI7
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_FI8
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_FI9
Number of Residues	4
Details	Modified residue: {"description":"N6-carboxylysine","evidences":[{"source":"UniProtKB","id":"P11498","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	4
Details	Modified residue: {"description":"N6-biotinyllysine","evidences":[{"source":"PROSITE-ProRule","id":"PRU01066","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	452
Details	Domain: {"description":"Biotin carboxylation","evidences":[{"source":"PROSITE-ProRule","id":"PRU00969","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	196
Details	Domain: {"description":"ATP-grasp","evidences":[{"source":"PROSITE-ProRule","id":"PRU00409","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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