Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1XKV

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

Replaces: 1WG9

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 2001

Chain	Residue
A	ARG130
A	ASN131
A	PHE133
A	GLY267
A	HOH3067
A	HOH3311

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA B 2002

Chain	Residue
B	GLY267
B	HOH4040
B	HOH4144
B	ARG130
B	ASN131
B	PHE133

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PO4 A 3001

Chain	Residue
A	VAL20
A	SER21
A	ARG130
A	ARG137
A	HOH3008
A	HOH3015
A	HOH3046
A	HOH3220
B	HIS38

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 A 3002

Chain	Residue
A	GLU259
A	LYS413
A	LYS416
A	HIS417
A	HOH3108

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PO4 B 3003

Chain	Residue
A	HIS38
A	HOH3037
A	HOH3047
A	HOH3221
B	SER21
B	PRO22
B	ARG130
B	ARG137

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 B 3004

Chain	Residue
B	LYS413
B	LYS416
B	HIS417
B	HOH4353

site_id	AC7
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PO4 B 3005

Chain	Residue
B	LEU233
B	SER234
B	GLY235
B	THR236
B	GLY237
B	LYS238
B	THR239
B	HOH4163
B	HOH4193
B	HOH4227
B	HOH4236
B	HOH4347

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PO4 B 3006

Chain	Residue
B	GLU5
B	HIS10
B	LYS12

site_id	AC9
Number of Residues	14
Details	BINDING SITE FOR RESIDUE ATP A 1001

Chain	Residue
A	LEU233
A	SER234
A	GLY235
A	THR236
A	GLY237
A	LYS238
A	THR239
A	THR240
A	LYS272
A	THR426
A	ARG438
A	PHE439
A	THR444
A	HOH3339

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL B 4001

Chain	Residue
B	PHE160
B	GLN161
B	ARG166
B	HOH4130
B	HOH4166
B	HOH4258

site_id	BC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL B 4002

Chain	Residue
A	GLU66
A	GLY67
A	TRP71
A	HOH3044
B	THR50
B	GLY51
B	THR315
B	HOH4058
B	HOH4064

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	12
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00453","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	6
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	2
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	2
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P22259","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	18
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	2
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	2
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	2
Details	Annotated By Reference To The Literature 1aq2

Chain	Residue	Details
A	HIS216
A	ARG319

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1aq2

Chain	Residue	Details
B	HIS216
B	ARG319

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