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1FBT

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 PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 A 300
ChainResidue
AARG7
AHIS8
AASN14
AARG57
AGLU77
AHIS142
AGLN143
AHOH360

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 B 191
ChainResidue
BHIS8
BASN14
BARG57
BGLU77
BHIS142
BGLN143
BHOH235
BARG7

Functional Information from PROSITE/UniProt
site_idPS00175
Number of Residues10
DetailsPG_MUTASE Phosphoglycerate mutase family phosphohistidine signature. LcRHGEsElN
ChainResidueDetails
ALEU5-ASN14

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Tele-phosphohistidine intermediate => ECO:0000269|PubMed:9253407
ChainResidueDetails
AGLY9
BGLY9

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:9253407
ChainResidueDetails
AILE78
BILE78

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q16875
ChainResidueDetails
AHIS8
ALEU15
ATHR58
AGLY180
BHIS8
BLEU15
BTHR58
BGLY180

site_idSWS_FT_FI4
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:9253407
ChainResidueDetails
AGLY21
BASP103
BTYR107
BGLU118
BALA144
BCYS148
AGLU89
AASP103
ATYR107
AGLU118
AALA144
ACYS148
BGLY21
BGLU89

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|Ref.15
ChainResidueDetails
AALA100
BALA100

site_idSWS_FT_FI6
Number of Residues2
DetailsSITE: Transition state stabilizer => ECO:0000250|UniProtKB:P00950
ChainResidueDetails
AGLN143
BGLN143

218853

PDB entries from 2024-04-24

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