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3E9C

Structure of a tryptic core fragment of TIGAR from Danio rerio

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004331molecular_functionfructose-2,6-bisphosphate 2-phosphatase activity
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005741cellular_componentmitochondrial outer membrane
A0005829cellular_componentcytosol
A0006914biological_processautophagy
A0006915biological_processapoptotic process
A0016787molecular_functionhydrolase activity
A0043456biological_processregulation of pentose-phosphate shunt
A0045820biological_processnegative regulation of glycolytic process
B0003824molecular_functioncatalytic activity
B0004331molecular_functionfructose-2,6-bisphosphate 2-phosphatase activity
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005741cellular_componentmitochondrial outer membrane
B0005829cellular_componentcytosol
B0006914biological_processautophagy
B0006915biological_processapoptotic process
B0016787molecular_functionhydrolase activity
B0043456biological_processregulation of pentose-phosphate shunt
B0045820biological_processnegative regulation of glycolytic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE K A 266
ChainResidue
ALEU202
APRO203
AHOH282
BVAL195
BGLU196
BLEU198

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K A 267
ChainResidue
BLEU202
BPRO203
AVAL195
AGLU196
ALEU198

Functional Information from PROSITE/UniProt
site_idPS00175
Number of Residues10
DetailsPG_MUTASE Phosphoglycerate mutase family phosphohistidine signature. IvRHGEtQyN
ChainResidueDetails
AILE8-ASN17

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Tele-phosphohistidine intermediate => ECO:0000269|PubMed:19015259
ChainResidueDetails
AHIS11
BHIS11

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:19015259
ChainResidueDetails
AGLU89
BGLU89

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Transition state stabilizer => ECO:0000305|PubMed:19015259
ChainResidueDetails
AHIS183
BHIS183

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1qhf
ChainResidueDetails
AARG61
AHIS183
AGLU89

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1qhf
ChainResidueDetails
BARG61
BHIS183
BGLU89

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PDB entries from 2024-07-17

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