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3GAY

Structure of Giardia fructose-1,6-biphosphate aldolase in complex with tagatose-1,6-biphosphate

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 326
ChainResidue
AHIS84
AHIS178
AHIS210
AP6T327

site_idAC2
Number of Residues24
DetailsBINDING SITE FOR RESIDUE P6T A 327
ChainResidue
AGLY179
ALYS182
AHIS210
AGLY211
ASER212
ASER213
AASN253
AVAL254
AASP255
ASER256
AARG259
AZN326
AHOH394
AHOH410
AHOH415
AHOH418
AHOH519
AHOH537
BARG280
AASN24
AGLN48
ASER50
AASP83
AHIS178

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 328
ChainResidue
BHIS84
BHIS178
BHIS210
BP6T329

site_idAC4
Number of Residues24
DetailsBINDING SITE FOR RESIDUE P6T B 329
ChainResidue
AARG280
BASN24
BGLN48
BSER50
BASP83
BHIS84
BHIS178
BGLY179
BLYS182
BHIS210
BGLY211
BSER212
BSER213
BASN253
BASP255
BSER256
BARG259
BZN328
BHOH350
BHOH388
BHOH477
BHOH558
BHOH574
BHOH610

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
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"19236002","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17166851","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19236002","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3GAY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3GB6","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17166851","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19236002","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21333622","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2ISV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ISW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3GAK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3GAY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3GB6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3OHI","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1b57
ChainResidueDetails
AASP83
AGLU143
AASN253

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1b57
ChainResidueDetails
BASP83
BGLU143
BASN253

249697

PDB entries from 2026-02-25

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