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1FZT

SOLUTION STRUCTURE AND DYNAMICS OF AN OPEN B-SHEET, GLYCOLYTIC ENZYME-MONOMERIC 23.7 KDA PHOSPHOGLYCERATE MUTASE FROM SCHIZOSACCHAROMYCES POMBE

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004619molecular_functionphosphoglycerate mutase activity
A0005634cellular_componentnucleus
A0005829cellular_componentcytosol
A0006094biological_processgluconeogenesis
A0006096biological_processglycolytic process
A0016853molecular_functionisomerase activity
A0016868molecular_functionintramolecular phosphotransferase activity
A0046538molecular_function2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity
A0061621biological_processcanonical glycolysis
Functional Information from PROSITE/UniProt
site_idPS00175
Number of Residues10
DetailsPG_MUTASE Phosphoglycerate mutase family phosphohistidine signature. LtRHGEsEwN
ChainResidueDetails
ALEU12-ASN21

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Tele-phosphohistidine intermediate => ECO:0000250|UniProtKB:P00950
ChainResidueDetails
AHIS15

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:P00950
ChainResidueDetails
AGLU93

site_idSWS_FT_FI3
Number of Residues7
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P00950
ChainResidueDetails
AARG14
ATHR27
AARG66
AGLU93
ALYS104
AARG120
AGLY164

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000250|UniProtKB:P00950
ChainResidueDetails
AHIS163

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:18257517
ChainResidueDetails
ATHR37

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:18257517
ChainResidueDetails
ASER62
ASER166

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:18257517
ChainResidueDetails
ATYR96

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1qhf
ChainResidueDetails
AHIS15
AGLU93
AARG66
AHIS163

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PDB entries from 2024-11-06

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