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3DCY

Crystal Structure a TP53-induced glycolysis and apoptosis regulator protein from Homo sapiens.

Functional Information from GO Data
ChainGOidnamespacecontents
A0002931biological_processresponse to ischemia
A0003824molecular_functioncatalytic activity
A0004331molecular_functionfructose-2,6-bisphosphate 2-phosphatase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005741cellular_componentmitochondrial outer membrane
A0005829cellular_componentcytosol
A0006914biological_processautophagy
A0006915biological_processapoptotic process
A0006950biological_processresponse to stress
A0006974biological_processDNA damage response
A0016787molecular_functionhydrolase activity
A0043067biological_processregulation of programmed cell death
A0043069biological_processnegative regulation of programmed cell death
A0043456biological_processregulation of pentose-phosphate shunt
A0045739biological_processpositive regulation of DNA repair
A0045820biological_processnegative regulation of glycolytic process
A0045937biological_processpositive regulation of phosphate metabolic process
A0071279biological_processcellular response to cobalt ion
A0071456biological_processcellular response to hypoxia
A1902153biological_processregulation of response to DNA damage checkpoint signaling
A1903301biological_processpositive regulation of hexokinase activity
A1905857biological_processpositive regulation of pentose-phosphate shunt
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 A 271
ChainResidue
AARG10
AHIS11
AASN17
AGLN23
AARG61
AGLU89
AHIS198
AGLY199

Functional Information from PROSITE/UniProt
site_idPS00175
Number of Residues10
DetailsPG_MUTASE Phosphoglycerate mutase family phosphohistidine signature. VvRHGEtRfN
ChainResidueDetails
AVAL8-ASN17

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Tele-phosphohistidine intermediate","evidences":[{"source":"UniProtKB","id":"Q7ZVE3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"Q7ZVE3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"UniProtKB","id":"Q7ZVE3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1qhf
ChainResidueDetails
AHIS198
AHIS11
AGLU89

246031

PDB entries from 2025-12-10

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