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3GB6

Structure of Giardia fructose-1,6-biphosphate aldolase D83A mutant in complex with fructose-1,6-bisphosphate

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
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
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 326
ChainResidue
AALA83
AHIS84
AHIS210
AASN253
AP6F327
AZN330

site_idAC2
Number of Residues26
DetailsBINDING SITE FOR RESIDUE P6F A 327
ChainResidue
AHIS178
AGLY179
ALYS182
AHIS210
AGLY211
ASER212
ASER213
AASN253
AVAL254
AASP255
ASER256
AARG259
AZN326
AZN330
AHOH371
AHOH403
AHOH436
AHOH449
AHOH471
AHOH525
AHOH553
AHOH611
BARG280
AASN24
AGLN48
ASER50

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 330
ChainResidue
AHIS84
AHIS178
AHIS210
AZN326
AP6F327

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 328
ChainResidue
BALA83
BHIS84
BHIS210
BP6F329
BZN331

site_idAC5
Number of Residues25
DetailsBINDING SITE FOR RESIDUE P6F B 329
ChainResidue
AARG280
BASN24
BGLN48
BSER50
BHIS178
BGLY179
BLYS182
BHIS210
BGLY211
BSER212
BSER213
BASN253
BASP255
BSER256
BARG259
BZN328
BZN331
BHOH382
BHOH413
BHOH447
BHOH461
BHOH468
BHOH534
BHOH545
BHOH568

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 331
ChainResidue
BHIS84
BHIS178
BHIS210
BZN328
BP6F329

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

246704

PDB entries from 2025-12-24

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