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3MOF

The structure of rat cytosolic PEPCK mutant A467G 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
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
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 Residues33
DetailsBINDING SITE FOR RESIDUE GTP A 900
ChainResidue
AHIS264
AASP311
AVAL335
APRO337
AGLY338
AARG405
AARG436
ATRP516
APHE517
APHE525
AGLY529
APRO285
APHE530
AASN533
AHOH628
AMN700
AHOH707
AHOH711
AHOH769
AHOH794
AMN800
AHOH802
ASER286
AHOH818
AHOH965
AOXL1000
AHOH1039
AALA287
ACYS288
AGLY289
ALYS290
ATHR291
AASN292

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 700
ChainResidue
ATHR291
AASP310
AHOH794
AHOH802
AHOH856
AGTP900

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN A 800
ChainResidue
ALYS244
AHIS264
AASP311
AGTP900
AOXL1000

site_idAC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE OXL A 1000
ChainResidue
AARG87
ALYS244
AHIS264
ASER286
AASP311
AARG405
AHOH631
AMN800
AHOH814
AGTP900
AHOH971

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 1100
ChainResidue
ALEU79
AASN208
AHOH840
AHOH940
AHOH1035

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE 1PE A 1200
ChainResidue
ALEU153
ATRP260
ALYS316
AARG324
AHOH876

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE 1PE A 1201
ChainResidue
AASN7
AASP10
APHE11
AALA13
ALYS14

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 3001
ChainResidue
AALA447
ASER449
APRO509
ALYS510
AILE511
AHOH906

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 3002
ChainResidue
APHE30
AASN34
ALYS191
AGLU227

site_idBC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO A 3003
ChainResidue
AARG543
ATYR557

site_idBC2
Number of Residues32
DetailsBINDING SITE FOR RESIDUE GTP B 1000
ChainResidue
BPHE530
BASN533
BHOH667
BMN700
BMN701
BHOH714
BHOH786
BHOH820
BHOH824
BHOH915
BHOH954
BHOH1027
BHOH1062
BHOH1077
BOXL1200
BHIS264
BPRO285
BSER286
BALA287
BCYS288
BGLY289
BLYS290
BTHR291
BASN292
BASP311
BVAL335
BARG405
BARG436
BTRP516
BPHE517
BPHE525
BGLY529

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN B 700
ChainResidue
BLYS244
BHIS264
BASP311
BGTP1000
BOXL1200

site_idBC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN B 701
ChainResidue
BTHR291
BHOH667
BHOH716
BHOH820
BGTP1000

site_idBC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA B 1100
ChainResidue
BLEU79
BASN208
BHOH766
BHOH883
BHOH930

site_idBC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE OXL B 1200
ChainResidue
BARG87
BLYS244
BHIS264
BSER286
BASP311
BARG405
BMN700
BHOH705
BHOH771
BGTP1000

site_idBC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE 1PE B 1300
ChainResidue
BASN7
BASP10
BALA13
BLYS14

site_idBC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 3000
ChainResidue
BALA447
BPRO509
BLYS510
BILE511
BHOH666
BHOH911

site_idBC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO B 3001
ChainResidue
BARG543
BTYR557

site_idCC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO B 3002
ChainResidue
BPHE30
BASN34
BGLU227

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

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PDB entries from 2024-07-10

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