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2P9T

Crystal Structure of Phosphoglycerate Kinase-2 bound to 3-phosphoglycerate

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
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE 3PG A 500
ChainResidue
AASP23
AHOH607
AHOH634
AHOH756
AHOH763
AASN25
AARG38
AHIS62
AARG65
AARG122
AGLY166
AARG170
AHOH580

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 Residues5
DetailsBINDING:
ChainResidueDetails
AASP23
AARG38
AHIS62
AARG122
AARG170

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:18004764
ChainResidueDetails
ALYS219
AGLY312
AGLU343
AGLY372

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P00558
ChainResidueDetails
ASER3

site_idSWS_FT_FI4
Number of Residues10
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P00558
ChainResidueDetails
ALYS10
ALYS290
ALYS47
ALYS74
ALYS85
ALYS96
ALYS130
ALYS145
ALYS198
ALYS266

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P00558
ChainResidueDetails
ATYR195

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 13pk
ChainResidueDetails
AARG38
ALYS215
AGLY373
AGLY396

222415

PDB entries from 2024-07-10

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