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2WZB

The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with ADP, 3PG and magnesium trifluoride

Functional Information from GO Data
ChainGOidnamespacecontents
A0004618molecular_functionphosphoglycerate kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006094biological_processgluconeogenesis
A0006096biological_processglycolytic process
A0016020cellular_componentmembrane
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0016525biological_processnegative regulation of angiogenesis
A0030855biological_processepithelial cell differentiation
A0031639biological_processplasminogen activation
A0043531molecular_functionADP binding
A0045121cellular_componentmembrane raft
A0047134molecular_functionprotein-disulfide reductase (NAD(P)H) activity
A0061621biological_processcanonical glycolysis
A0070062cellular_componentextracellular exosome
A0071456biological_processcellular response to hypoxia
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 1417
ChainResidue
AASP374
AADP1419
AMGF1421
AHOH2608
AHOH2614

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 1418
ChainResidue
AARG65
ALYS215
AASP218
AHOH2362

site_idAC3
Number of Residues29
DetailsBINDING SITE FOR RESIDUE ADP A 1419
ChainResidue
AGLY213
AALA214
ALYS215
ALYS219
AGLY237
AGLY238
ALEU256
AGLY312
AASN336
APRO338
AGLY340
AVAL341
AGLU343
AGLY371
AGLY372
AGLY373
AASP374
ATHR375
AMG1417
AMGF1421
AHOH2527
AHOH2557
AHOH2608
AHOH2609
AHOH2610
AHOH2611
AHOH2612
AHOH2613
AHOH2614

site_idAC4
Number of Residues15
DetailsBINDING SITE FOR RESIDUE 3PG A 1420
ChainResidue
AASP23
AASN25
AARG38
AHIS62
AARG65
AARG122
AGLY166
AARG170
ALYS215
AMGF1421
AHOH2303
AHOH2614
AHOH2615
AHOH2616
AHOH2617

site_idAC5
Number of Residues13
DetailsBINDING SITE FOR RESIDUE MGF A 1421
ChainResidue
AARG38
ALYS215
ALYS219
AGLY372
AGLY373
AGLY395
AGLY396
AMG1417
AADP1419
A3PG1420
AHOH2608
AHOH2614
AHOH2617

Functional Information from PROSITE/UniProt
site_idPS00111
Number of Residues11
DetailsPGLYCERATE_KINASE Phosphoglycerate kinase signature. RVVMRvDfNVP
ChainResidueDetails
AARG17-PRO27

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues9
DetailsBINDING: BINDING => ECO:0000269|PubMed:18463139
ChainResidueDetails
AASP23
AARG38
AHIS62
AARG122
AARG170
ALYS219
AGLY312
AGLU343
AGLY372

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER1
ASER3

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P09411
ChainResidueDetails
ALYS5
ALYS190

site_idSWS_FT_FI4
Number of Residues7
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS10
ALYS74
ALYS85
ALYS145
ALYS198
ALYS266
ALYS290

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P09411
ChainResidueDetails
ALYS47

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P09411
ChainResidueDetails
ATYR75

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P09411
ChainResidueDetails
ALYS90
ALYS360

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS96

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: N6-malonyllysine; alternate => ECO:0000269|PubMed:21908771
ChainResidueDetails
ALYS130

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455
ChainResidueDetails
ATYR195

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER202

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:29775581
ChainResidueDetails
ALYS215
ALYS322

site_idSWS_FT_FI13
Number of Residues1
DetailsMOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:29192674
ChainResidueDetails
ALYS219

219140

PDB entries from 2024-05-01

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