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4GNL

Structure of rat cytosolic PEPCK Ld_2g in complex with PEP and GDP

Functional Information from GO Data
ChainGOidnamespacecontents
A0004611molecular_functionphosphoenolpyruvate carboxykinase activity
A0004613molecular_functionphosphoenolpyruvate carboxykinase (GTP) activity
A0005525molecular_functionGTP binding
A0006094biological_processgluconeogenesis
A0017076molecular_functionpurine nucleotide binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 701
ChainResidue
ALYS244
AHIS264
AASP311
AHOH803
AHOH804
AHOH805

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MN A 702
ChainResidue
AHOH1147
ATHR291
AHOH1145
AHOH1146

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 703
ChainResidue
ALEU79
AASN208
AHOH880
AHOH886
AHOH1082

site_idAC4
Number of Residues21
DetailsBINDING SITE FOR RESIDUE GDP A 704
ChainResidue
APRO285
AALA287
ACYS288
AGLY289
ALYS290
ATHR291
AASN292
AARG436
ATRP516
APHE517
APHE525
AGLY529
APHE530
AASN533
AHOH801
AHOH802
AHOH843
AHOH863
AHOH1057
AHOH1144
AHOH1147

site_idAC5
Number of Residues13
DetailsBINDING SITE FOR RESIDUE PEP A 705
ChainResidue
AALA86
AARG87
ATYR235
AGLY236
AGLY237
ALYS244
AASN403
AARG405
APHE485
AHOH803
AHOH804
AHOH806
AHOH868

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 Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:30193097
ChainResidueDetails
ALYS521
ALYS524

224931

PDB entries from 2024-09-11

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