Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4HNT

crystal structure of F403A mutant of S. aureus Pyruvate carboxylase

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	15
Details	BINDING SITE FOR RESIDUE ADP A 1201

Chain	Residue
A	LYS152
A	GLN268
A	GLU311
A	LEU313
A	ILE323
A	GLU324
A	THR478
A	ILE167
A	MET192
A	LYS194
A	SER197
A	GLU236
A	ARG237
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	7
Details	BINDING SITE FOR RESIDUE BTI A 1203

Chain	Residue
A	ASN506
A	ASN510
A	GLY511
A	PHE512
A	PRO513
A	PHE618
A	LYS620

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE BTI B 1201

Chain	Residue
B	ASN506
B	GLY511
B	PRO513
B	LYS620

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN B 1202

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	17
Details	BINDING SITE FOR RESIDUE ATP C 1202

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

site_id	AC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE BTI D 1201

Chain	Residue
D	TYR503
D	ASN506
D	ASN510
D	GLY511
D	PHE512
D	PRO513
D	PHE618
D	LYS620
D	PHE1038

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN D 1202

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)