Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3C3C

Crystal Structure of human phosphoglycerate kinase bound to 3-phosphoglycerate and L-CDP

Functional Information from GO Data
ChainGOidnamespacecontents
A0004618molecular_functionphosphoglycerate kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0005759cellular_componentmitochondrial matrix
A0005829cellular_componentcytosol
A0006094biological_processgluconeogenesis
A0006096biological_processglycolytic process
A0016020cellular_componentmembrane
A0016301molecular_functionkinase activity
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
A0160218
B0004618molecular_functionphosphoglycerate kinase activity
B0004674molecular_functionprotein serine/threonine kinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005615cellular_componentextracellular space
B0005737cellular_componentcytoplasm
B0005759cellular_componentmitochondrial matrix
B0005829cellular_componentcytosol
B0006094biological_processgluconeogenesis
B0006096biological_processglycolytic process
B0016020cellular_componentmembrane
B0016301molecular_functionkinase activity
B0016525biological_processnegative regulation of angiogenesis
B0030855biological_processepithelial cell differentiation
B0031639biological_processplasminogen activation
B0043531molecular_functionADP binding
B0045121cellular_componentmembrane raft
B0047134molecular_functionprotein-disulfide reductase (NAD(P)H) activity
B0061621biological_processcanonical glycolysis
B0070062cellular_componentextracellular exosome
B0071456biological_processcellular response to hypoxia
B0160218
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE 3PG A 418
ChainResidue
AASP23
AASN25
AARG38
AHIS62
AARG65
AARG122
AGLY166
ATHR167
AARG170

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 3PG B 417
ChainResidue
BASP23
BASN25
BARG38
BHIS62
BARG65
BARG122
BGLY166
BARG170

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE CDP A 419
ChainResidue
AGLY213
AALA214
ALYS219
AGLY237
AGLY238
AGLY312
ALEU313
APRO338
AGLY340
AGLU343

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 Residues18
DetailsBINDING: BINDING => ECO:0000269|PubMed:18463139
ChainResidueDetails
AASP23
BASP23
BARG38
BHIS62
BARG122
BARG170
BLYS219
BGLY312
BGLU343
BGLY372
AARG38
AHIS62
AARG122
AARG170
ALYS219
AGLY312
AGLU343
AGLY372

site_idSWS_FT_FI2
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER1
ASER3
BSER1
BSER3

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P09411
ChainResidueDetails
ALYS5
ALYS190
BLYS5
BLYS190

site_idSWS_FT_FI4
Number of Residues14
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS10
BLYS85
BLYS145
BLYS198
BLYS266
BLYS290
ALYS74
ALYS85
ALYS145
ALYS198
ALYS266
ALYS290
BLYS10
BLYS74

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P09411
ChainResidueDetails
ALYS47
BLYS47

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P09411
ChainResidueDetails
ATYR75
BTYR75

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P09411
ChainResidueDetails
ALYS90
ALYS360
BLYS90
BLYS360

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS96
BLYS96

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: N6-malonyllysine; alternate => ECO:0000269|PubMed:21908771
ChainResidueDetails
ALYS130
BLYS130

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455
ChainResidueDetails
ATYR195
BTYR195

site_idSWS_FT_FI11
Number of Residues2
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
BSER202

site_idSWS_FT_FI12
Number of Residues4
DetailsMOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:29775581
ChainResidueDetails
ALYS215
ALYS322
BLYS215
BLYS322

site_idSWS_FT_FI13
Number of Residues2
DetailsMOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:29192674
ChainResidueDetails
ALYS219
BLYS219

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 13pk
ChainResidueDetails
AARG38
ALYS215
AGLY396

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 13pk
ChainResidueDetails
BARG38
BLYS215
BGLY396

227111

PDB entries from 2024-11-06

PDB statisticsPDBj update infoContact PDBjnumon