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3DT2

The structure of rat cytosolic PEPCK in complex with oxalate and GTP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004550molecular_functionnucleoside diphosphate kinase activity
A0004611molecular_functionphosphoenolpyruvate carboxykinase activity
A0004613molecular_functionphosphoenolpyruvate carboxykinase (GTP) activity
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005783cellular_componentendoplasmic reticulum
A0005829cellular_componentcytosol
A0006006biological_processglucose metabolic process
A0006094biological_processgluconeogenesis
A0006107biological_processoxaloacetate metabolic process
A0006629biological_processlipid metabolic process
A0009617biological_processresponse to bacterium
A0014823biological_processresponse to activity
A0016301molecular_functionkinase activity
A0016831molecular_functioncarboxy-lyase activity
A0017076molecular_functionpurine nucleotide binding
A0018105biological_processpeptidyl-serine phosphorylation
A0019003molecular_functionGDP binding
A0019543biological_processpropionate catabolic process
A0030145molecular_functionmanganese ion binding
A0031406molecular_functioncarboxylic acid binding
A0031667biological_processresponse to nutrient levels
A0032496biological_processresponse to lipopolysaccharide
A0032868biological_processresponse to insulin
A0032869biological_processcellular response to insulin stimulus
A0033993biological_processresponse to lipid
A0042593biological_processglucose homeostasis
A0042594biological_processresponse to starvation
A0043382biological_processpositive regulation of memory T cell differentiation
A0043648biological_processdicarboxylic acid metabolic process
A0045944biological_processpositive regulation of transcription by RNA polymerase II
A0046166biological_processglyceraldehyde-3-phosphate biosynthetic process
A0046327biological_processglycerol biosynthetic process from pyruvate
A0046872molecular_functionmetal ion binding
A0046889biological_processpositive regulation of lipid biosynthetic process
A0046890biological_processregulation of lipid biosynthetic process
A0051365biological_processcellular response to potassium ion starvation
A0070365biological_processhepatocyte differentiation
A0070741biological_processresponse to interleukin-6
A0071300biological_processcellular response to retinoic acid
A0071320biological_processcellular response to cAMP
A0071332biological_processcellular response to fructose stimulus
A0071333biological_processcellular response to glucose stimulus
A0071347biological_processcellular response to interleukin-1
A0071356biological_processcellular response to tumor necrosis factor
A0071377biological_processcellular response to glucagon stimulus
A0071456biological_processcellular response to hypoxia
A0071474biological_processcellular hyperosmotic response
A0071475biological_processcellular hyperosmotic salinity response
A0071476biological_processcellular hypotonic response
A0071477biological_processcellular hypotonic salinity response
A0071549biological_processcellular response to dexamethasone stimulus
A0072350biological_processtricarboxylic acid metabolic process
A0097403biological_processcellular response to raffinose
A0106264molecular_functionprotein serine kinase activity (using GTP as donor)
A1904628biological_processcellular response to phorbol 13-acetate 12-myristate
A1904640biological_processresponse to methionine
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MN A 700
ChainResidue
ATHR291
AHOH1179
AHOH1194
AHOH1242

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MN A 701
ChainResidue
ALYS244
AHIS264
AASP311

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE OXL A 800
ChainResidue
AHIS264
ASER286
AASP311
AARG405
AALA467
AHOH1140
AHOH1168
AHOH1198
AARG87
ALYS244

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 1000
ChainResidue
ALEU79
AASN208
AHOH1217
AHOH1261
AHOH1422

site_idAC5
Number of Residues29
DetailsBINDING SITE FOR RESIDUE GTP A 900
ChainResidue
AHIS264
APRO285
ASER286
AALA287
ACYS288
AGLY289
ALYS290
ATHR291
AASN292
AASP311
APRO337
AARG405
AARG436
ATRP516
APHE517
APHE525
AGLY529
APHE530
AASN533
AHOH1114
AHOH1128
AHOH1172
AHOH1174
AHOH1179
AHOH1186
AHOH1197
AHOH1227
AHOH1242
AHOH1350

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE 1PE A 1100
ChainResidue
ALEU153
ATRP260
ATRP314
AMET315
ALYS316
AARG324
AGLU424
AHOH1477
AHOH1513

Functional Information from PROSITE/UniProt
site_idPS00505
Number of Residues9
DetailsPEPCK_GTP Phosphoenolpyruvate carboxykinase (GTP) signature. FPSACGKTN
ChainResidueDetails
APHE284-ASN292

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:23127136, ECO:0000269|PubMed:2909519
ChainResidueDetails
ACYS288

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:17685635, ECO:0000269|PubMed:18772387, ECO:0000269|PubMed:20476774, ECO:0000269|PubMed:23127136, ECO:0000269|PubMed:24863970
ChainResidueDetails
AARG87

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:18197707, ECO:0000269|PubMed:18772387, ECO:0000269|PubMed:20476774, ECO:0000269|PubMed:23127136, ECO:0000269|PubMed:24863970
ChainResidueDetails
ATYR235
AASN403

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: 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
ChainResidueDetails
ALYS244
AHIS264
AASP311

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: 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
ChainResidueDetails
ASER286

site_idSWS_FT_FI6
Number of Residues3
DetailsBINDING: 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
ChainResidueDetails
AALA287
AARG436
APHE530

site_idSWS_FT_FI7
Number of Residues1
DetailsBINDING: 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
ChainResidueDetails
AARG405

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903
ChainResidueDetails
ASER19
ASER118

site_idSWS_FT_FI9
Number of Residues3
DetailsMOD_RES: N6-acetyllysine; by p300/EP300 => ECO:0000250|UniProtKB:P35558
ChainResidueDetails
ALYS70
ALYS71
ALYS594

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P35558
ChainResidueDetails
ASER90

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; by p300/EP300 => ECO:0000250|UniProtKB:P35558, ECO:0000269|PubMed:30193097
ChainResidueDetails
ALYS91

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q16822
ChainResidueDetails
ATHR178

site_idSWS_FT_FI13
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q16822
ChainResidueDetails
ASER286

site_idSWS_FT_FI14
Number of Residues3
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:30193097
ChainResidueDetails
ALYS473
ALYS521
ALYS524

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1aq2
ChainResidueDetails
AHIS264
ALYS290
AARG405

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1aq2
ChainResidueDetails
AHIS264
AARG405

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PDB entries from 2024-05-01

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