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

2P9Q

Crystal Structure of Phosphoglycerate Kinase-2

Functional Information from GO Data
ChainGOidnamespacecontents
A0004618molecular_functionphosphoglycerate kinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005929cellular_componentcilium
A0006094biological_processgluconeogenesis
A0006096biological_processglycolytic process
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0030317biological_processflagellated sperm motility
A0035686cellular_componentsperm fibrous sheath
A0043531molecular_functionADP binding
B0004618molecular_functionphosphoglycerate kinase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005929cellular_componentcilium
B0006094biological_processgluconeogenesis
B0006096biological_processglycolytic process
B0016301molecular_functionkinase activity
B0016310biological_processphosphorylation
B0030317biological_processflagellated sperm motility
B0035686cellular_componentsperm fibrous sheath
B0043531molecular_functionADP binding
Functional Information from PROSITE/UniProt
site_idPS00111
Number of Residues11
DetailsPGLYCERATE_KINASE Phosphoglycerate kinase signature. RVIMRvDfNVP
ChainResidueDetails
AARG17-PRO27

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING:
ChainResidueDetails
AASP23
BARG170
AARG38
AHIS62
AARG122
AARG170
BASP23
BARG38
BHIS62
BARG122

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:18004764
ChainResidueDetails
ALYS219
AGLY312
AGLU343
AGLY372
BLYS219
BGLY312
BGLU343
BGLY372

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P00558
ChainResidueDetails
ASER3
BSER3

site_idSWS_FT_FI4
Number of Residues20
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P00558
ChainResidueDetails
ALYS10
ALYS290
BLYS10
BLYS47
BLYS74
BLYS85
BLYS96
BLYS130
BLYS145
BLYS198
BLYS266
ALYS47
BLYS290
ALYS74
ALYS85
ALYS96
ALYS130
ALYS145
ALYS198
ALYS266

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P00558
ChainResidueDetails
ATYR195
BTYR195

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

222415

PDB entries from 2024-07-10

PDB statisticsPDBj update infoContact PDBjnumon