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3GAK

Structure of Giardia fructose-1,6-biphosphate aldolase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004332molecular_functionfructose-bisphosphate aldolase activity
A0005515molecular_functionprotein binding
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
B0005515molecular_functionprotein binding
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
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 331
ChainResidue
AHIS84
AMET103
AGLU135
AHIS210

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN B 332
ChainResidue
BHIS84
BHIS178
BHIS210

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 327
ChainResidue
ASER213
AASN253
AASP255
ASER256
AGLY211
ASER212

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 328
ChainResidue
ASER50
AARG259
BARG280

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 329
ChainResidue
BGLY179
BLYS182
BGLY211
BSER212
BSER213
BASP255
BSER256

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 330
ChainResidue
AARG280
BSER50
BARG259

Functional Information from PROSITE/UniProt
site_idPS00806
Number of Residues12
DetailsALDOLASE_CLASS_II_2 Fructose-bisphosphate aldolase class-II signature 2. VEaELGtlGGiE
ChainResidueDetails
AVAL132-GLU143

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:19236002, ECO:0000305|PubMed:17166851
ChainResidueDetails
AASP83
BASP83

site_idSWS_FT_FI2
Number of Residues20
DetailsBINDING: BINDING => ECO:0000269|PubMed:19236002, ECO:0007744|PDB:3GAY, ECO:0007744|PDB:3GB6
ChainResidueDetails
ASER50
AARG280
BSER50
BGLY179
BLYS182
BGLY211
BSER213
BASN253
BASP255
BSER256
BARG259
AGLY179
BARG280
ALYS182
AGLY211
ASER213
AASN253
AASP255
ASER256
AARG259

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:17166851, ECO:0000269|PubMed:19236002, ECO:0000269|PubMed:21333622, ECO:0007744|PDB:2ISV, ECO:0007744|PDB:2ISW, ECO:0007744|PDB:3GAK, ECO:0007744|PDB:3GAY, ECO:0007744|PDB:3GB6, ECO:0007744|PDB:3OHI
ChainResidueDetails
AHIS84
AHIS178
AHIS210
BHIS84
BHIS178
BHIS210

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1b57
ChainResidueDetails
AASP83
AASN253

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1b57
ChainResidueDetails
BASP83
BASN253

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PDB entries from 2024-07-24

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