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4DEL

Active site loop dynamics of a class IIa fructose 1,6-bisphosphate aldolase from M. tuberculosis

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 Residues6
DetailsBINDING SITE FOR RESIDUE NA A 401
ChainResidue
AVAL211
AGLY213
AGLY253
ASER255
APGH404
AHOH588

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 402
ChainResidue
APGH404
AHIS96
AHIS212
AHIS252

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 403
ChainResidue
AGLU198
AHIS199
AHIS344
AHIS346
AHOH992

site_idAC4
Number of Residues17
DetailsBINDING SITE FOR RESIDUE PGH A 404
ChainResidue
AASN27
AASP95
AHIS96
AHIS212
AGLY213
AHIS252
AGLY253
AGLY254
ASER255
AASN274
AVAL275
AASP276
ATHR277
ANA401
AZN402
AHOH557
AHOH823

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE ACT A 405
ChainResidue
ALEU13
AGLY14
ALYS17
ALYS201
AASP248
AP6G406
AHOH829
AHOH866

site_idAC6
Number of Residues14
DetailsBINDING SITE FOR RESIDUE P6G A 406
ChainResidue
AALA10
AGLU11
AASP138
ALYS189
AALA196
AGLY197
ALYS201
ATYR202
AACT405
AHOH646
AHOH866
AHOH935
AHOH960
AHOH969

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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