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3LL4

Structure of the H13A mutant of Ykr043C in complex with fructose-1,6-bisphosphate

Functional Information from GO Data
ChainGOidnamespacecontents
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0016491molecular_functionoxidoreductase activity
A0016787molecular_functionhydrolase activity
A0046390biological_processribose phosphate biosynthetic process
A0050278molecular_functionsedoheptulose-bisphosphatase activity
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0016491molecular_functionoxidoreductase activity
B0016787molecular_functionhydrolase activity
B0046390biological_processribose phosphate biosynthetic process
B0050278molecular_functionsedoheptulose-bisphosphatase activity
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE 2FP A 301
ChainResidue
AARG12
AHIS178
AARG181
AHOH279
AHOH281
BHIS244
ASER19
ATYR24
ATHR25
AARG69
AGLU99
ATYR102
AHIS176
AGLY177

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE 2FP B 301
ChainResidue
AHIS244
BARG12
BSER19
BTYR24
BTHR25
BARG69
BGLU99
BTYR102
BHIS176
BGLY177
BHIS178
BARG181

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Tele-phosphohistidine intermediate => ECO:0000269|PubMed:20427268
ChainResidueDetails
AALA13
BALA13

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:20427268
ChainResidueDetails
AGLU99
BGLU99

site_idSWS_FT_FI3
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:20427268
ChainResidueDetails
AARG12
BGLU99
BARG181
BHIS244
ATYR24
AARG69
AGLU99
AARG181
AHIS244
BARG12
BTYR24
BARG69

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Transition state stabilizer => ECO:0000305|PubMed:20427268
ChainResidueDetails
AHIS176
BHIS176

223532

PDB entries from 2024-08-07

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