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3EKL

Structural Characterization of tetrameric Mycobacterium tuberculosis fructose 1,6-bisphosphate aldolase - substrate binding and catalysis mechanism of a class IIa bacterial aldolase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004332molecular_functionfructose-bisphosphate aldolase activity
A0005576cellular_componentextracellular region
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0005975biological_processcarbohydrate metabolic process
A0006094biological_processgluconeogenesis
A0006096biological_processglycolytic process
A0008270molecular_functionzinc ion binding
A0009274cellular_componentpeptidoglycan-based cell wall
A0016829molecular_functionlyase activity
A0016832molecular_functionaldehyde-lyase activity
A0035375molecular_functionzymogen binding
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE 13P A 350
ChainResidue
AASN27
AVAL275
AASP276
ATHR277
AZN352
ANA354
AHOH413
AASP95
AHIS212
AGLY213
AHIS252
AGLY253
AGLY254
ASER255
AASN274

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE 13P A 351
ChainResidue
AASN27
AASP95
AHIS96
AHIS212
AGLY213
AHIS252
AGLY253
AGLY254
ASER255
AASN274
AVAL275
AASP276
ATHR277
AZN352
ANA354
AHOH413

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 352
ChainResidue
AHIS96
AHIS212
AHIS252
A13P350
A13P351

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 353
ChainResidue
AGLU198
AHIS199
AHIS344
AHIS346
AHOH459

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NA A 354
ChainResidue
AVAL211
AGLY213
AGLY253
ASER255
A13P350
A13P351
AHOH638

Functional Information from PROSITE/UniProt
site_idPS00602
Number of Residues12
DetailsALDOLASE_CLASS_II_1 Fructose-bisphosphate aldolase class-II signature 1. Yp..VNVa.LHtDHC
ChainResidueDetails
ATYR86-CYS97

site_idPS00806
Number of Residues12
DetailsALDOLASE_CLASS_II_2 Fructose-bisphosphate aldolase class-II signature 2. LEiEIGvvGGeE
ChainResidueDetails
ALEU158-GLU169

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
AASP95

site_idSWS_FT_FI2
Number of Residues9
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ASER53
AHIS96
AASP131
AGLU161
AHIS212
AGLY213
AHIS252
AGLY253
AASN274

218853

PDB entries from 2024-04-24

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