Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3QM3

1.85 Angstrom Resolution Crystal Structure of Fructose-bisphosphate Aldolase (Fba) from Campylobacter jejuni

Functional Information from GO Data
ChainGOidnamespacecontents
A0004332molecular_functionfructose-bisphosphate aldolase activity
A0005829cellular_componentcytosol
A0005975biological_processcarbohydrate metabolic process
A0006094biological_processgluconeogenesis
A0006096biological_processglycolytic process
A0008270molecular_functionzinc ion binding
A0016829molecular_functionlyase activity
A0016832molecular_functionaldehyde-lyase activity
A0046872molecular_functionmetal ion binding
B0004332molecular_functionfructose-bisphosphate aldolase activity
B0005829cellular_componentcytosol
B0005975biological_processcarbohydrate metabolic process
B0006094biological_processgluconeogenesis
B0006096biological_processglycolytic process
B0008270molecular_functionzinc ion binding
B0016829molecular_functionlyase activity
B0016832molecular_functionaldehyde-lyase activity
B0046872molecular_functionmetal ion binding
C0004332molecular_functionfructose-bisphosphate aldolase activity
C0005829cellular_componentcytosol
C0005975biological_processcarbohydrate metabolic process
C0006094biological_processgluconeogenesis
C0006096biological_processglycolytic process
C0008270molecular_functionzinc ion binding
C0016829molecular_functionlyase activity
C0016832molecular_functionaldehyde-lyase activity
C0046872molecular_functionmetal ion binding
D0004332molecular_functionfructose-bisphosphate aldolase activity
D0005829cellular_componentcytosol
D0005975biological_processcarbohydrate metabolic process
D0006094biological_processgluconeogenesis
D0006096biological_processglycolytic process
D0008270molecular_functionzinc ion binding
D0016829molecular_functionlyase activity
D0016832molecular_functionaldehyde-lyase activity
D0046872molecular_functionmetal ion binding
E0004332molecular_functionfructose-bisphosphate aldolase activity
E0005829cellular_componentcytosol
E0005975biological_processcarbohydrate metabolic process
E0006094biological_processgluconeogenesis
E0006096biological_processglycolytic process
E0008270molecular_functionzinc ion binding
E0016829molecular_functionlyase activity
E0016832molecular_functionaldehyde-lyase activity
E0046872molecular_functionmetal ion binding
F0004332molecular_functionfructose-bisphosphate aldolase activity
F0005829cellular_componentcytosol
F0005975biological_processcarbohydrate metabolic process
F0006094biological_processgluconeogenesis
F0006096biological_processglycolytic process
F0008270molecular_functionzinc ion binding
F0016829molecular_functionlyase activity
F0016832molecular_functionaldehyde-lyase activity
F0046872molecular_functionmetal ion binding
G0004332molecular_functionfructose-bisphosphate aldolase activity
G0005829cellular_componentcytosol
G0005975biological_processcarbohydrate metabolic process
G0006094biological_processgluconeogenesis
G0006096biological_processglycolytic process
G0008270molecular_functionzinc ion binding
G0016829molecular_functionlyase activity
G0016832molecular_functionaldehyde-lyase activity
G0046872molecular_functionmetal ion binding
H0004332molecular_functionfructose-bisphosphate aldolase activity
H0005829cellular_componentcytosol
H0005975biological_processcarbohydrate metabolic process
H0006094biological_processgluconeogenesis
H0006096biological_processglycolytic process
H0008270molecular_functionzinc ion binding
H0016829molecular_functionlyase activity
H0016832molecular_functionaldehyde-lyase activity
H0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 355
ChainResidue
AHIS105
AGLU169
AHIS221
AHIS260
AHOH362

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT A 356
ChainResidue
AHOH2887
AGLY10
AVAL11
AHIS89
AHOH2006

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 357
ChainResidue
ALYS86
AHIS128
AHOH2539
AHOH2806
BLYS86

site_idAC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE SO4 A 358
ChainResidue
AGLY261
AGLY262
ASER263
AASN282
AILE283
AASP284
ATHR285
AHOH1366
AHOH1552
AHOH3395
AHOH3504

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 355
ChainResidue
BHIS105
BGLU169
BHIS221
BHIS260
BHOH2086

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 356
ChainResidue
BGLY10
BVAL11
BHIS89
BTYR124
BHOH1484

site_idAC7
Number of Residues12
DetailsBINDING SITE FOR RESIDUE GOL B 357
ChainResidue
BASN282
BILE283
BASP284
BTHR285
BHOH1066
BHOH1533
BHOH1794
BHOH1936
BHOH2194
BHOH2637
BHOH3600
BHOH3601

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 358
ChainResidue
AARG327
AHOH1263
BSER61
BHOH520
BHOH1614
BHOH1796
BHOH1965

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 359
ChainResidue
ASER61
AHOH3479
BARG327
BHOH385
BHOH1328
BHOH3219
BHOH3553

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 360
ChainResidue
AARG331
AGLU335
BLYS71
BASN72
GLYS109

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN C 355
ChainResidue
CHIS105
CGLU169
CHIS221
CHIS260
CHOH371

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL C 356
ChainResidue
CGLY10
CVAL11
CHIS89
CHOH2502
CHOH2960
CHOH3374

site_idBC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 C 357
ChainResidue
CARG327
CHOH400
CHOH891
CHOH1374
CHOH1945
DSER61

site_idBC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 C 358
ChainResidue
CSER61
CHOH408
CHOH922
CHOH1865
CHOH3280
CHOH3602
DARG327

site_idBC6
Number of Residues11
DetailsBINDING SITE FOR RESIDUE SO4 C 359
ChainResidue
CHOH1461
CHOH2299
CHOH3131
CGLY261
CGLY262
CSER263
CASN282
CILE283
CASP284
CTHR285
CHOH1252

site_idBC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN D 355
ChainResidue
DHIS105
DGLU169
DHIS221
DHIS260
DHOH375

site_idBC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL D 356
ChainResidue
DSER263
DILE283
DASP284
DTHR285
DASP286

site_idBC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT D 357
ChainResidue
DGLY10
DVAL11
DHIS89
DGLN130
DHOH1874

site_idCC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FMT D 358
ChainResidue
DTHR285
DSO4360
DHOH2054
DHOH3154

site_idCC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 D 359
ChainResidue
CARG331
CGLU335
DLYS71
DASN72
DHOH3096
ELYS109

site_idCC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 D 360
ChainResidue
DSER263
DASN282
DILE283
DASP284
DTHR285
DFMT358
DHOH1240
DHOH1540
DHOH2249
DHOH3599

site_idCC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN E 355
ChainResidue
EHIS105
EGLU169
EHIS221
EHIS260
EHOH367

site_idCC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL E 356
ChainResidue
EGLY10
EVAL11
EHIS89
EHOH1481
EHOH2386
EHOH2674

site_idCC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 E 357
ChainResidue
EARG327
EHOH376
EHOH821
EHOH1871
EHOH2383
EHOH3548
FSER61
FHOH1301

site_idCC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 E 358
ChainResidue
ESER61
EASN62
EGLY63
EHOH1392
EHOH1777
EHOH2196
EHOH2558
FARG327

site_idCC8
Number of Residues11
DetailsBINDING SITE FOR RESIDUE SO4 E 359
ChainResidue
EGLY261
EGLY262
ESER263
EASN282
EILE283
EASP284
ETHR285
EHOH1245
EHOH1505
EHOH1831
EHOH2147

site_idCC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 E 360
ChainResidue
EHIS128
EHOH3581
FLYS86

site_idDC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN F 355
ChainResidue
FHIS105
FGLU169
FHIS221
FHIS260
FHOH2367

site_idDC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FMT F 356
ChainResidue
FGLY10
FVAL11
FHIS89
FGLN130
FHOH2298
FHOH2416
FHOH3337

site_idDC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL F 357
ChainResidue
FGLY261
FSER263
FASN282
FILE283
FASP284
FTHR285
FHOH2103
FHOH3186
FHOH3191
FHOH3596

site_idDC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 F 358
ChainResidue
CLYS109
EARG331
EGLU335
FLYS71
FASN72

site_idDC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN G 355
ChainResidue
GHIS105
GGLU169
GHIS221
GHIS260
GHOH379

site_idDC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 G 356
ChainResidue
GARG327
GHOH408
GHOH1222
GHOH1296
GHOH1897
GHOH2443
HSER61
HHOH1901

site_idDC7
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 G 357
ChainResidue
GGLY261
GGLY262
GSER263
GASN282
GILE283
GASP284
GTHR285
GHOH1405
GHOH2072
GHOH3512

site_idDC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 G 358
ChainResidue
GLYS86
GHIS128
GHOH3554
HLYS86

site_idDC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 G 359
ChainResidue
GGLY10
GVAL11
GHIS89
GLYS93
GGLN130
GHOH1682
GHOH2258
GHOH3542

site_idEC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN H 355
ChainResidue
HHIS105
HGLU169
HHIS221
HHIS260
HHOH504

site_idEC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT H 356
ChainResidue
HGLY10
HVAL11
HHIS89
HHOH1934
HHOH3256

site_idEC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 H 357
ChainResidue
GSER61
HARG327
HHOH369
HHOH377

site_idEC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 H 358
ChainResidue
ALYS109
GARG331
GGLU335
HLYS71
HASN72
HHOH3257

Functional Information from PROSITE/UniProt
site_idPS00602
Number of Residues12
DetailsALDOLASE_CLASS_II_1 Fructose-bisphosphate aldolase class-II signature 1. Yg..VPVi.LHtDHA
ChainResidueDetails
ATYR95-ALA106

site_idPS00806
Number of Residues12
DetailsALDOLASE_CLASS_II_2 Fructose-bisphosphate aldolase class-II signature 2. LEiELGctGGeE
ChainResidueDetails
ALEU166-GLU177

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
AASP104
BASP104
CASP104
DASP104
EASP104
FASP104
GASP104
HASP104

site_idSWS_FT_FI2
Number of Residues72
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ASER61
BSER61
BHIS105
BASP139
BGLU169
BHIS221
BGLY222
BHIS260
BGLY261
BASN282
CSER61
AHIS105
CHIS105
CASP139
CGLU169
CHIS221
CGLY222
CHIS260
CGLY261
CASN282
DSER61
DHIS105
AASP139
DASP139
DGLU169
DHIS221
DGLY222
DHIS260
DGLY261
DASN282
ESER61
EHIS105
EASP139
AGLU169
EGLU169
EHIS221
EGLY222
EHIS260
EGLY261
EASN282
FSER61
FHIS105
FASP139
FGLU169
AHIS221
FHIS221
FGLY222
FHIS260
FGLY261
FASN282
GSER61
GHIS105
GASP139
GGLU169
GHIS221
AGLY222
GGLY222
GHIS260
GGLY261
GASN282
HSER61
HHIS105
HASP139
HGLU169
HHIS221
HGLY222
AHIS260
HHIS260
HGLY261
HASN282
AGLY261
AASN282

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon