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1TIP

THE BISPHOSPHATASE DOMAIN OF THE BIFUNCTIONAL RAT LIVER 6-PHOSPHOFRUCTO-2-KINASE/FRUCTOSE-2,6-BISPHOSPHATASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005524molecular_functionATP binding
A0006003biological_processfructose 2,6-bisphosphate metabolic process
B0003824molecular_functioncatalytic activity
B0005524molecular_functionATP binding
B0006003biological_processfructose 2,6-bisphosphate metabolic process
Functional Information from PROSITE/UniProt
site_idPS00175
Number of Residues10
DetailsPG_MUTASE Phosphoglycerate mutase family phosphohistidine signature. LcRHGEsElN
ChainResidueDetails
ALEU6-ASN15

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Tele-phosphohistidine intermediate => ECO:0000269|PubMed:9253407
ChainResidueDetails
AGLY10
BGLY10

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:9253407
ChainResidueDetails
AILE79
BILE79

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q16875
ChainResidueDetails
ANEP9
ALEU16
ATHR59
AGLY181
BNEP9
BLEU16
BTHR59
BGLY181

site_idSWS_FT_FI4
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:9253407
ChainResidueDetails
AGLY22
BASP104
BTYR108
BGLU119
BALA145
BCYS149
AGLU90
AASP104
ATYR108
AGLU119
AALA145
ACYS149
BGLY22
BGLU90

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|Ref.15
ChainResidueDetails
AALA101
BALA101

site_idSWS_FT_FI6
Number of Residues2
DetailsSITE: Transition state stabilizer => ECO:0000250|UniProtKB:P00950
ChainResidueDetails
AGLN144
BGLN144

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1qhf
ChainResidueDetails
AARG58
AHIS143
AGLU78

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1qhf
ChainResidueDetails
BARG58
BHIS143
BGLU78

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PDB entries from 2024-11-06

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