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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1J3B

Crystal structure of ATP-dependent phosphoenolpyruvate carboxykinase from Thermus thermophilus HB8

Functional Information from GO Data

Chain	GOid	namespace	contents
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	0006094	biological_process	gluconeogenesis
A	0016831	molecular_function	carboxy-lyase activity
A	0017076	molecular_function	purine nucleotide binding
A	0046872	molecular_function	metal ion 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	0006094	biological_process	gluconeogenesis
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	5
Details	BINDING SITE FOR RESIDUE CA A 1001

Chain	Residue
A	ARG130
A	ASN131
A	PHE133
A	GLY267
A	HOH3030

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA B 1002

Chain	Residue
B	HOH3104
B	ARG130
B	ASN131
B	PHE133
B	GLY267

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PO4 A 2001

Chain	Residue
A	VAL20
A	SER21
A	ARG130
A	ARG137
A	HOH3016
A	HOH3020
A	HOH3028
B	HIS38

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 A 2002

Chain	Residue
A	LYS413
A	LYS416
A	HIS417
A	HOH3145

site_id	AC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PO4 A 2003

Chain	Residue
A	LEU233
A	SER234
A	GLY235
A	THR236
A	GLY237
A	LYS238
A	THR239
A	LYS272
A	HOH3176
A	HOH3286

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PO4 A 2004

Chain	Residue
A	ARG340
A	HOH3045
A	HOH3190

site_id	AC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PO4 B 2005

Chain	Residue
A	HIS38
A	HOH3040
A	HOH3052
A	HOH3127
B	SER21
B	PRO22
B	ARG130
B	ARG137
B	HOH3261

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 B 2006

Chain	Residue
B	GLU259
B	LYS413
B	LYS416
B	HIS417
B	HOH3310

site_id	AC9
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PO4 B 2007

Chain	Residue
B	LEU233
B	SER234
B	GLY235
B	THR236
B	GLY237
B	LYS238
B	THR239
B	HOH3178
B	HOH3184
B	HOH3246
B	HOH3248

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 B 2008

Chain	Residue
B	GLU5
B	HIS10
B	LYS12
B	HOH3314

site_id	BC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PO4 B 2009

Chain	Residue
B	ARG111
B	ARG210

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 3001

Chain	Residue
A	TYR93
A	GLN161
A	ARG166
A	HOH3164

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL B 3002

Chain	Residue
B	PHE160
B	GLN161
B	ARG166
B	HOH3097
B	HOH3243

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: BINDING => ECO:0000255\|HAMAP-Rule:MF_00453

Chain	Residue	Details
A	ARG52
B	ASP253
B	GLU281
B	ARG319
A	TYR191
A	LYS197
A	ASP253
A	GLU281
A	ARG319
B	ARG52
B	TYR191
B	LYS197

site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269\|PubMed:16239727, ECO:0000269\|Ref.3, ECO:0007744\|PDB:1J3B, ECO:0007744\|PDB:1XKV, ECO:0007744\|PDB:2PC9

Chain	Residue	Details
A	ARG130
A	ASN131
A	GLY267
B	ARG130
B	ASN131
B	GLY267

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:16239727, ECO:0000269\|Ref.3, ECO:0007744\|PDB:1J3B, ECO:0007744\|PDB:2PC9

Chain	Residue	Details
A	PHE133
B	PHE133

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:P22259

Chain	Residue	Details
A	HIS216
B	HIS216

site_id	SWS_FT_FI5
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00453, ECO:0000269\|PubMed:16239727, ECO:0000269\|Ref.3, ECO:0007744\|PDB:1XKV, ECO:0007744\|PDB:2PC9

Chain	Residue	Details
A	GLY232
A	THR444
B	GLY232
B	THR444

site_id	SWS_FT_FI6
Number of Residues	2
Details	BINDING: BINDING => ECO:0000305\|PubMed:16239727, ECO:0000305\|Ref.3, ECO:0007744\|PDB:1XKV, ECO:0007744\|PDB:2PC9

Chain	Residue	Details
A	ARG438
B	ARG438

site_id	SWS_FT_FI7
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00453, ECO:0000269\|PubMed:16239727, ECO:0000269\|Ref.3

Chain	Residue	Details
A	PHE439
B	PHE439

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

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