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2RK8

The Structure of rat cytosolic PEPCK in complex with phosphonoformate

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
A0016310biological_processphosphorylation
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
B0000287molecular_functionmagnesium ion binding
B0004550molecular_functionnucleoside diphosphate kinase activity
B0004611molecular_functionphosphoenolpyruvate carboxykinase activity
B0004613molecular_functionphosphoenolpyruvate carboxykinase (GTP) activity
B0005525molecular_functionGTP binding
B0005737cellular_componentcytoplasm
B0005783cellular_componentendoplasmic reticulum
B0005829cellular_componentcytosol
B0006006biological_processglucose metabolic process
B0006094biological_processgluconeogenesis
B0006107biological_processoxaloacetate metabolic process
B0006629biological_processlipid metabolic process
B0009617biological_processresponse to bacterium
B0014823biological_processresponse to activity
B0016301molecular_functionkinase activity
B0016310biological_processphosphorylation
B0016831molecular_functioncarboxy-lyase activity
B0017076molecular_functionpurine nucleotide binding
B0018105biological_processpeptidyl-serine phosphorylation
B0019003molecular_functionGDP binding
B0019543biological_processpropionate catabolic process
B0030145molecular_functionmanganese ion binding
B0031406molecular_functioncarboxylic acid binding
B0031667biological_processresponse to nutrient levels
B0032496biological_processresponse to lipopolysaccharide
B0032868biological_processresponse to insulin
B0032869biological_processcellular response to insulin stimulus
B0033993biological_processresponse to lipid
B0042593biological_processglucose homeostasis
B0042594biological_processresponse to starvation
B0043382biological_processpositive regulation of memory T cell differentiation
B0043648biological_processdicarboxylic acid metabolic process
B0045944biological_processpositive regulation of transcription by RNA polymerase II
B0046166biological_processglyceraldehyde-3-phosphate biosynthetic process
B0046327biological_processglycerol biosynthetic process from pyruvate
B0046872molecular_functionmetal ion binding
B0046889biological_processpositive regulation of lipid biosynthetic process
B0046890biological_processregulation of lipid biosynthetic process
B0051365biological_processcellular response to potassium ion starvation
B0070365biological_processhepatocyte differentiation
B0070741biological_processresponse to interleukin-6
B0071300biological_processcellular response to retinoic acid
B0071320biological_processcellular response to cAMP
B0071332biological_processcellular response to fructose stimulus
B0071333biological_processcellular response to glucose stimulus
B0071347biological_processcellular response to interleukin-1
B0071356biological_processcellular response to tumor necrosis factor
B0071377biological_processcellular response to glucagon stimulus
B0071456biological_processcellular response to hypoxia
B0071474biological_processcellular hyperosmotic response
B0071475biological_processcellular hyperosmotic salinity response
B0071476biological_processcellular hypotonic response
B0071477biological_processcellular hypotonic salinity response
B0071549biological_processcellular response to dexamethasone stimulus
B0072350biological_processtricarboxylic acid metabolic process
B0097403biological_processcellular response to raffinose
B0106264molecular_functionprotein serine kinase activity (using GTP as donor)
B1904628biological_processcellular response to phorbol 13-acetate 12-myristate
B1904640biological_processresponse to methionine
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN A 700
ChainResidue
ALYS244
AHIS264
AASP311
APPF3969
AHOH5803

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 624
ChainResidue
AHOH5930
AHOH6047
AVAL65
ALEU79
AASN208
AHOH5839

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN B 700
ChainResidue
BLYS244
BHIS264
BASP311
BPPF3969
BHOH4040

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA B 624
ChainResidue
BLEU79
BASN208
BHOH3970
BHOH4138
BHOH4249

site_idAC5
Number of Residues13
DetailsBINDING SITE FOR RESIDUE PPF A 3969
ChainResidue
AARG87
ALYS244
AHIS264
ASER286
AASP311
APHE333
AARG405
AMN700
AHOH5786
AHOH5803
AHOH5924
AHOH5943
AHOH6055

site_idAC6
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PPF B 3969
ChainResidue
BARG87
BLYS244
BHIS264
BSER286
BASP311
BARG405
BMN700
BHOH4040
BHOH4161
BHOH4203
BHOH4257
BHOH4360

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FMT A 3406
ChainResidue
AALA287
AGLY289
AARG436
AHOH5914

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PEG A 5759
ChainResidue
AASN7
AASP10
APHE11
ALYS14
AGLN39
AHOH6143

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FMT B 3406
ChainResidue
BTYR235
BGLY236
BGLY237
BASN403
BARG405
BHOH4257

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 Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:23127136, ECO:0000269|PubMed:2909519
ChainResidueDetails
ACYS288
BCYS288

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:17685635, ECO:0000269|PubMed:18772387, ECO:0000269|PubMed:20476774, ECO:0000269|PubMed:23127136, ECO:0000269|PubMed:24863970
ChainResidueDetails
AARG87
BARG87

site_idSWS_FT_FI3
Number of Residues4
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
BTYR235
BASN403

site_idSWS_FT_FI4
Number of Residues6
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
BLYS244
BHIS264
BASP311

site_idSWS_FT_FI5
Number of Residues2
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
BSER286

site_idSWS_FT_FI6
Number of Residues6
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
BALA287
BARG436
BPHE530

site_idSWS_FT_FI7
Number of Residues2
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
BARG405

site_idSWS_FT_FI8
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903
ChainResidueDetails
ASER19
ASER118
BSER19
BSER118

site_idSWS_FT_FI9
Number of Residues6
DetailsMOD_RES: N6-acetyllysine; by p300/EP300 => ECO:0000250|UniProtKB:P35558
ChainResidueDetails
ALYS70
ALYS71
ALYS594
BLYS70
BLYS71
BLYS594

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P35558
ChainResidueDetails
ASER90
BSER90

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: N6-acetyllysine; by p300/EP300 => ECO:0000250|UniProtKB:P35558, ECO:0000269|PubMed:30193097
ChainResidueDetails
ALYS91
BLYS91

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q16822
ChainResidueDetails
ATHR178
BTHR178

site_idSWS_FT_FI13
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q16822
ChainResidueDetails
ASER286
BSER286

site_idSWS_FT_FI14
Number of Residues6
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:30193097
ChainResidueDetails
ALYS473
ALYS521
ALYS524
BLYS473
BLYS521
BLYS524

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

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1aq2
ChainResidueDetails
BHIS264
BLYS290
BARG405

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1aq2
ChainResidueDetails
AHIS264
AARG405

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1aq2
ChainResidueDetails
BHIS264
BARG405

226707

PDB entries from 2024-10-30

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