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2PAA

Crystal structure of phosphoglycerate kinase-2 bound to atp and 3pg

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 PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE ATP A 500
ChainResidue
AGLY212
AASN336
AGLY337
APRO338
AGLY340
AVAL341
AGLU343
AGLY373
AASP374
ATHR375
AGLY213
AALA214
ALYS219
AGLY237
AGLY238
ALEU256
AGLY312
ALEU313

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE 3PG B 501
ChainResidue
BHIS62
BARG122
BGLY166
BARG170

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
AHIS62
AARG122
AARG170
BASP23
BARG38
BHIS62
BARG122
BARG170
AASP23
AARG38

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

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
ALYS74
ALYS85
ALYS96
ALYS130
ALYS145
ALYS198
ALYS266
ALYS290
BLYS10
BLYS47
BLYS74
BLYS85
BLYS96
BLYS130
BLYS145
BLYS198
BLYS266
BLYS290
ALYS10
ALYS47

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

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PDB entries from 2024-06-12

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