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2FJK

Crystal structure of Fructose-1,6-Bisphosphate Aldolase in Thermus caldophilus

Functional Information from GO Data
ChainGOidnamespacecontents
A0004332molecular_functionfructose-bisphosphate aldolase activity
A0005975biological_processcarbohydrate metabolic process
A0006096biological_processglycolytic process
A0008270molecular_functionzinc ion binding
A0016829molecular_functionlyase activity
A0016832molecular_functionaldehyde-lyase activity
A0030388biological_processfructose 1,6-bisphosphate metabolic process
A0046872molecular_functionmetal ion binding
B0004332molecular_functionfructose-bisphosphate aldolase activity
B0005975biological_processcarbohydrate metabolic process
B0006096biological_processglycolytic process
B0008270molecular_functionzinc ion binding
B0016829molecular_functionlyase activity
B0016832molecular_functionaldehyde-lyase activity
B0030388biological_processfructose 1,6-bisphosphate metabolic process
B0046872molecular_functionmetal ion binding
C0004332molecular_functionfructose-bisphosphate aldolase activity
C0005975biological_processcarbohydrate metabolic process
C0006096biological_processglycolytic process
C0008270molecular_functionzinc ion binding
C0016829molecular_functionlyase activity
C0016832molecular_functionaldehyde-lyase activity
C0030388biological_processfructose 1,6-bisphosphate metabolic process
C0046872molecular_functionmetal ion binding
D0004332molecular_functionfructose-bisphosphate aldolase activity
D0005975biological_processcarbohydrate metabolic process
D0006096biological_processglycolytic process
D0008270molecular_functionzinc ion binding
D0016829molecular_functionlyase activity
D0016832molecular_functionaldehyde-lyase activity
D0030388biological_processfructose 1,6-bisphosphate metabolic process
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE 13P A 1063
ChainResidue
AASP80
AASN251
AASP253
ATHR254
AHIS81
AHIS178
AGLY179
ALYS182
AHIS208
AGLY209
AALA210
ASER211

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE 13P B 1073
ChainResidue
BASN23
BASP80
BHIS81
BHIS178
BGLY179
BLYS182
BHIS208
BGLY209
BALA210
BSER211
BASN251
BASP253
BTHR254
BHOH1086

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE 13P C 1083
ChainResidue
CASP80
CHIS81
CHIS178
CGLY179
CLYS182
CHIS208
CGLY209
CALA210
CSER211
CASN251
CASP253
CTHR254
CHOH1130

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE 13P D 1093
ChainResidue
DASP80
DHIS81
DHIS178
DLYS182
DHIS208
DGLY209
DALA210
DSER211
DASN251
DTHR252
DASP253
DTHR254

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues48
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1b57
ChainResidueDetails
AASP80
AASN251
AGLU140

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1b57
ChainResidueDetails
BASP80
BASN251
BGLU147

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1b57
ChainResidueDetails
CASP80
CASN251
CGLU140

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1b57
ChainResidueDetails
DASP80
DASN251

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PDB entries from 2025-12-17

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