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3OHI

Structure of Giardia fructose-1,6-biphosphate aldolase in complex with 3-hydroxy-2-pyridone

Functional Information from GO Data
ChainGOidnamespacecontents
A0004332molecular_functionfructose-bisphosphate aldolase activity
A0005515molecular_functionprotein binding
A0005829cellular_componentcytosol
A0005975biological_processcarbohydrate metabolic process
A0006096biological_processglycolytic process
A0008270molecular_functionzinc ion binding
A0009025molecular_functiontagatose-bisphosphate aldolase activity
A0016829molecular_functionlyase activity
A0016832molecular_functionaldehyde-lyase activity
A0046872molecular_functionmetal ion binding
B0004332molecular_functionfructose-bisphosphate aldolase activity
B0005515molecular_functionprotein binding
B0005829cellular_componentcytosol
B0005975biological_processcarbohydrate metabolic process
B0006096biological_processglycolytic process
B0008270molecular_functionzinc ion binding
B0009025molecular_functiontagatose-bisphosphate aldolase activity
B0016829molecular_functionlyase activity
B0016832molecular_functionaldehyde-lyase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 340
ChainResidue
AHIS84
AHIS178
AHIS210
AHDX341

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE HDX A 341
ChainResidue
AGLY179
ALYS182
AGLY211
ASER212
ASER213
AASN253
AASP255
ASER256
AARG259
AZN340
AHOH389
BARG280
AASN24
ASER50
AASP83
AHIS84
AHIS178

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 342
ChainResidue
BHIS84
BHIS178
BHIS210
BHDX343

site_idAC4
Number of Residues18
DetailsBINDING SITE FOR RESIDUE HDX B 343
ChainResidue
AARG280
BASN24
BGLN48
BSER50
BASP83
BHIS84
BHIS178
BGLY179
BLYS182
BGLY211
BSER212
BSER213
BASN253
BASP255
BSER256
BARG259
BZN342
BHOH420

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

218853

PDB entries from 2024-04-24

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