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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4GMM

Structure of rat cytosolic PEPCK Ld_1g in complex with Beta-Sulfopyruvate and GTP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004611	molecular_function	phosphoenolpyruvate carboxykinase activity
A	0004613	molecular_function	phosphoenolpyruvate carboxykinase (GTP) activity
A	0005525	molecular_function	GTP binding
A	0006094	biological_process	gluconeogenesis
A	0017076	molecular_function	purine nucleotide binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	32
Details	BINDING SITE FOR RESIDUE GTP A 701

Chain	Residue
A	HIS264
A	ASP311
A	VAL335
A	ARG405
A	ARG436
A	TRP516
A	PHE517
A	PHE525
A	GLY529
A	PHE530
A	ASN533
A	PRO285
A	MN703
A	MN704
A	SPV705
A	HOH801
A	HOH803
A	HOH842
A	HOH850
A	HOH873
A	HOH888
A	HOH967
A	SER286
A	HOH1020
A	HOH1021
A	HOH1068
A	ALA287
A	CYS288
A	GLY289
A	LYS290
A	THR291
A	ASN292

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA A 702

Chain	Residue
A	LEU79
A	ASN208
A	HOH804
A	HOH805
A	HOH1055

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN A 703

Chain	Residue
A	LYS244
A	HIS264
A	ASP311
A	GTP701
A	SPV705

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN A 704

Chain	Residue
A	THR291
A	GTP701
A	HOH801
A	HOH802
A	HOH803

site_id	AC5
Number of Residues	15
Details	BINDING SITE FOR RESIDUE SPV A 705

Chain	Residue
A	ARG87
A	GLY236
A	GLY237
A	LYS243
A	LYS244
A	HIS264
A	SER286
A	ASP311
A	PHE333
A	ARG405
A	GTP701
A	MN703
A	HOH809
A	HOH810
A	HOH814

Functional Information from PROSITE/UniProt

site_id	PS00505
Number of Residues	9
Details	PEPCK_GTP Phosphoenolpyruvate carboxykinase (GTP) signature. FPSACGKTN

Chain	Residue	Details
A	PHE284-ASN292

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: ACT_SITE => ECO:0000269\|PubMed:23127136, ECO:0000269\|PubMed:2909519

Chain	Residue	Details
A	CYS288

site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269\|PubMed:17685635, ECO:0000269\|PubMed:18772387, ECO:0000269\|PubMed:20476774, ECO:0000269\|PubMed:23127136, ECO:0000269\|PubMed:24863970

Chain	Residue	Details
A	ARG87

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:18197707, ECO:0000269\|PubMed:18772387, ECO:0000269\|PubMed:20476774, ECO:0000269\|PubMed:23127136, ECO:0000269\|PubMed:24863970

Chain	Residue	Details
A	TYR235
A	ASN403

site_id	SWS_FT_FI4
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269\|PubMed:17685635, ECO:0000269\|PubMed:18197707, ECO:0000269\|PubMed:18772387, ECO:0000269\|PubMed:20476774, ECO:0000269\|PubMed:23127136, ECO:0000269\|PubMed:24863970, ECO:0000269\|PubMed:26322521, ECO:0000269\|PubMed:26709450, ECO:0000269\|PubMed:28345895, ECO:0000269\|PubMed:31461616, ECO:0007744\|PDB:4YW9, ECO:0007744\|PDB:5FH0, ECO:0007744\|PDB:5FH1, ECO:0007744\|PDB:5FH2, ECO:0007744\|PDB:5FH3, ECO:0007744\|PDB:5FH4, ECO:0007744\|PDB:5FH5, ECO:0007744\|PDB:5V97, ECO:0007744\|PDB:5V9F, ECO:0007744\|PDB:5V9G, ECO:0007744\|PDB:6P5O

Chain	Residue	Details
A	LYS244
A	HIS264
A	ASP311

site_id	SWS_FT_FI5
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269\|PubMed:17685635, ECO:0000269\|PubMed:18197707, ECO:0000269\|PubMed:18772387, ECO:0000269\|PubMed:20476774, ECO:0000269\|PubMed:23127136, ECO:0000269\|PubMed:24863970

Chain	Residue	Details
A	SER286

site_id	SWS_FT_FI6
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269\|PubMed:17685635, ECO:0000269\|PubMed:18772387, ECO:0000269\|PubMed:20476774, ECO:0000269\|PubMed:23127136, ECO:0000269\|PubMed:24863970, ECO:0000269\|PubMed:26322521, ECO:0000269\|PubMed:26709450, ECO:0000269\|PubMed:28345895, ECO:0007744\|PDB:4YW9, ECO:0007744\|PDB:5FH0, ECO:0007744\|PDB:5FH1, ECO:0007744\|PDB:5FH2, ECO:0007744\|PDB:5FH3, ECO:0007744\|PDB:5FH4, ECO:0007744\|PDB:5V97, ECO:0007744\|PDB:5V9F, ECO:0007744\|PDB:5V9G

Chain	Residue	Details
A	ALA287
A	ARG436
A	PHE530

site_id	SWS_FT_FI7
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269\|PubMed:17685635, ECO:0000269\|PubMed:20476774, ECO:0000269\|PubMed:23127136, ECO:0000269\|PubMed:24863970, ECO:0000269\|PubMed:26322521, ECO:0000269\|PubMed:26709450, ECO:0000269\|PubMed:28345895, ECO:0007744\|PDB:4YW9, ECO:0007744\|PDB:5FH0, ECO:0007744\|PDB:5FH1, ECO:0007744\|PDB:5FH2, ECO:0007744\|PDB:5FH3, ECO:0007744\|PDB:5FH4, ECO:0007744\|PDB:5V97, ECO:0007744\|PDB:5V9F, ECO:0007744\|PDB:5V9G

Chain	Residue	Details
A	ARG405

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:22673903

Chain	Residue	Details
A	SER19
A	SER118

site_id	SWS_FT_FI9
Number of Residues	3
Details	MOD_RES: N6-acetyllysine; by p300/EP300 => ECO:0000250\|UniProtKB:P35558

Chain	Residue	Details
A	LYS70
A	LYS71
A	LYS594

site_id	SWS_FT_FI10
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:P35558

Chain	Residue	Details
A	SER90

site_id	SWS_FT_FI11
Number of Residues	1
Details	MOD_RES: N6-acetyllysine; by p300/EP300 => ECO:0000250\|UniProtKB:P35558, ECO:0000269\|PubMed:30193097

Chain	Residue	Details
A	LYS91

site_id	SWS_FT_FI12
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0000250\|UniProtKB:Q16822

Chain	Residue	Details
A	THR178

site_id	SWS_FT_FI13
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:Q16822

Chain	Residue	Details
A	SER286

site_id	SWS_FT_FI14
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0000269\|PubMed:30193097

Chain	Residue	Details
A	LYS521
A	LYS524

223532

PDB entries from 2024-08-07

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