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2Q8M

T-like Fructose-1,6-bisphosphatase from Escherichia coli with AMP, Glucose 6-phosphate, and Fructose 1,6-bisphosphate bound

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005975biological_processcarbohydrate metabolic process
A0005986biological_processsucrose biosynthetic process
A0006000biological_processfructose metabolic process
A0006002biological_processfructose 6-phosphate metabolic process
A0006094biological_processgluconeogenesis
A0016787molecular_functionhydrolase activity
A0016791molecular_functionphosphatase activity
A0030388biological_processfructose 1,6-bisphosphate metabolic process
A0032991cellular_componentprotein-containing complex
A0042132molecular_functionfructose 1,6-bisphosphate 1-phosphatase activity
A0042578molecular_functionphosphoric ester hydrolase activity
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005975biological_processcarbohydrate metabolic process
B0005986biological_processsucrose biosynthetic process
B0006000biological_processfructose metabolic process
B0006002biological_processfructose 6-phosphate metabolic process
B0006094biological_processgluconeogenesis
B0016787molecular_functionhydrolase activity
B0016791molecular_functionphosphatase activity
B0030388biological_processfructose 1,6-bisphosphate metabolic process
B0032991cellular_componentprotein-containing complex
B0042132molecular_functionfructose 1,6-bisphosphate 1-phosphatase activity
B0042578molecular_functionphosphoric ester hydrolase activity
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS00124
Number of Residues13
DetailsFBPASE Fructose-1-6-bisphosphatase active site. GKLrlLYEcnPMA
ChainResidueDetails
AGLY268-ALA280

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01855, ECO:0000269|PubMed:17567577
ChainResidueDetails
AGLU89
ALEU112
BGLU89
BLEU112

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01855, ECO:0000269|PubMed:17567577, ECO:0000269|PubMed:17933867
ChainResidueDetails
AASP110
AASP113
AGLU275
BASP110
BASP113
BGLU275

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01855, ECO:0000305|PubMed:17314096, ECO:0000305|PubMed:17567577
ChainResidueDetails
AASN206
ATYR239
ATYR257
ALYS269
BASN206
BTYR239
BTYR257
BLYS269

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305|PubMed:17314096, ECO:0007744|PDB:2OX3
ChainResidueDetails
ATHR3
ALYS30
BTHR3
BLYS30

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:17567577, ECO:0007744|PDB:2Q8M
ChainResidueDetails
ATHR19
ALYS104
BTHR19
BLYS104

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:17314096, ECO:0000305|PubMed:17933867, ECO:0007744|PDB:2OWZ, ECO:0007744|PDB:2QVR
ChainResidueDetails
APHE187
BPHE187

site_idSWS_FT_FI7
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305|PubMed:17567577, ECO:0007744|PDB:2Q8M
ChainResidueDetails
ALYS222
AGLN225
BLYS222
BGLN225

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1eyi
ChainResidueDetails
AGLU90

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1eyi
ChainResidueDetails
BGLU90

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PDB entries from 2024-07-10

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