Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2PC9

Crystal Structure Of ATP-Dependent Phosphoenolpyruvate Carboxykinase From Thermus thermophilus HB8

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0004611	molecular_function	phosphoenolpyruvate carboxykinase activity
A	0004612	molecular_function	phosphoenolpyruvate carboxykinase (ATP) activity
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006094	biological_process	gluconeogenesis
A	0016829	molecular_function	lyase activity
A	0016831	molecular_function	carboxy-lyase activity
A	0017076	molecular_function	purine nucleotide binding
A	0046872	molecular_function	metal ion binding
B	0000166	molecular_function	nucleotide binding
B	0004611	molecular_function	phosphoenolpyruvate carboxykinase activity
B	0004612	molecular_function	phosphoenolpyruvate carboxykinase (ATP) activity
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006094	biological_process	gluconeogenesis
B	0016829	molecular_function	lyase activity
B	0016831	molecular_function	carboxy-lyase activity
B	0017076	molecular_function	purine nucleotide binding
B	0046872	molecular_function	metal ion binding
C	0000166	molecular_function	nucleotide binding
C	0004611	molecular_function	phosphoenolpyruvate carboxykinase activity
C	0004612	molecular_function	phosphoenolpyruvate carboxykinase (ATP) activity
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006094	biological_process	gluconeogenesis
C	0016829	molecular_function	lyase activity
C	0016831	molecular_function	carboxy-lyase activity
C	0017076	molecular_function	purine nucleotide binding
C	0046872	molecular_function	metal ion binding
D	0000166	molecular_function	nucleotide binding
D	0004611	molecular_function	phosphoenolpyruvate carboxykinase activity
D	0004612	molecular_function	phosphoenolpyruvate carboxykinase (ATP) activity
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006094	biological_process	gluconeogenesis
D	0016829	molecular_function	lyase activity
D	0016831	molecular_function	carboxy-lyase activity
D	0017076	molecular_function	purine nucleotide binding
D	0046872	molecular_function	metal ion binding

Functional Information from PROSITE/UniProt

site_id	PS00532
Number of Residues	16
Details	PEPCK_ATP Phosphoenolpyruvate carboxykinase (ATP) signature. LIGDDEHgWsEdGVfN

Chain	Residue	Details
A	LEU249-ASN264

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00453","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16239727","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"OCT-2007","submissionDatabase":"PDB data bank","title":"Crystal structure of ATP-dependent phosphoenolpyruvate carboxykinase from Thermus thermophilus HB8.","authoringGroup":["RIKEN structural genomics initiative (RSGI)"]}},{"source":"PDB","id":"1J3B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XKV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2PC9","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16239727","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"OCT-2007","submissionDatabase":"PDB data bank","title":"Crystal structure of ATP-dependent phosphoenolpyruvate carboxykinase from Thermus thermophilus HB8.","authoringGroup":["RIKEN structural genomics initiative (RSGI)"]}},{"source":"PDB","id":"1J3B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2PC9","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P22259","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	36
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00453","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16239727","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"OCT-2007","submissionDatabase":"PDB data bank","title":"Crystal structure of ATP-dependent phosphoenolpyruvate carboxykinase from Thermus thermophilus HB8.","authoringGroup":["RIKEN structural genomics initiative (RSGI)"]}},{"source":"PDB","id":"1XKV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2PC9","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16239727","evidenceCode":"ECO:0000305"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"OCT-2007","submissionDatabase":"PDB data bank","title":"Crystal structure of ATP-dependent phosphoenolpyruvate carboxykinase from Thermus thermophilus HB8.","authoringGroup":["RIKEN structural genomics initiative (RSGI)"]}},{"source":"PDB","id":"1XKV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2PC9","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00453","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16239727","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"OCT-2007","submissionDatabase":"PDB data bank","title":"Crystal structure of ATP-dependent phosphoenolpyruvate carboxykinase from Thermus thermophilus HB8.","authoringGroup":["RIKEN structural genomics initiative (RSGI)"]}}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1aq2

Chain	Residue	Details
A	HIS216
A	ARG319
A	LYS238

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1aq2

Chain	Residue	Details
B	HIS216
B	ARG319
B	LYS238

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1aq2

Chain	Residue	Details
C	HIS216
C	ARG319
C	LYS238

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1aq2

Chain	Residue	Details
D	HIS216
D	ARG319
D	LYS238

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1aq2

Chain	Residue	Details
A	HIS216
A	ARG319

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1aq2

Chain	Residue	Details
B	HIS216
B	ARG319

site_id	CSA7
Number of Residues	2
Details	Annotated By Reference To The Literature 1aq2

Chain	Residue	Details
C	HIS216
C	ARG319

site_id	CSA8
Number of Residues	2
Details	Annotated By Reference To The Literature 1aq2

Chain	Residue	Details
D	HIS216
D	ARG319

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