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1DOS

STRUCTURE OF FRUCTOSE-BISPHOSPHATE ALDOLASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004332molecular_functionfructose-bisphosphate aldolase activity
A0005515molecular_functionprotein binding
A0005829cellular_componentcytosol
A0005975biological_processcarbohydrate metabolic process
A0006094biological_processgluconeogenesis
A0006096biological_processglycolytic process
A0008270molecular_functionzinc ion binding
A0016829molecular_functionlyase activity
A0016832molecular_functionaldehyde-lyase activity
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0046872molecular_functionmetal ion binding
B0004332molecular_functionfructose-bisphosphate aldolase activity
B0005515molecular_functionprotein binding
B0005829cellular_componentcytosol
B0005975biological_processcarbohydrate metabolic process
B0006094biological_processgluconeogenesis
B0006096biological_processglycolytic process
B0008270molecular_functionzinc ion binding
B0016829molecular_functionlyase activity
B0016832molecular_functionaldehyde-lyase activity
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE ZN A 1005
ChainResidue
AHIS110
AGLU174
AHIS226
AHIS264
AHOH1116
AHOH1122
AHOH1291
AHOH1433

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NH4 A 1006
ChainResidue
AHIS107
AASP109
AMET142
AGLU172
AHIS264
ALYS284
AASN286
AGLN59

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ZN B 1323
ChainResidue
BHIS110
BGLU174
BHIS226
BHIS264
BHOH1782
BHOH1783
BHOH1793

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NH4 B 1324
ChainResidue
BGLN59
BHIS107
BASP109
BGLU172
BLYS284
BASN286

Functional Information from PROSITE/UniProt
site_idPS00602
Number of Residues12
DetailsALDOLASE_CLASS_II_1 Fructose-bisphosphate aldolase class-II signature 1. Yg..VPVi.LHtDHC
ChainResidueDetails
ATYR100-CYS111

site_idPS00806
Number of Residues12
DetailsALDOLASE_CLASS_II_2 Fructose-bisphosphate aldolase class-II signature 2. LEiELGctGGeE
ChainResidueDetails
ALEU171-GLU182

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:10080900
ChainResidueDetails
AHIS110
BHIS110

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
AASN62
BASN62

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:10080900, ECO:0000269|PubMed:8836102, ECO:0000269|PubMed:8939754
ChainResidueDetails
ACYS111
BGLY265
ALEU145
ALEU175
AGLY227
AGLY265
BCYS111
BLEU145
BLEU175
BGLY227

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING:
ChainResidueDetails
AVAL228
AGLY266
AILE287
BVAL228
BGLY266
BILE287

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:21151122
ChainResidueDetails
APRO9
BPRO9

site_idSWS_FT_FI6
Number of Residues14
DetailsMOD_RES: N6-succinyllysine => ECO:0000269|PubMed:21151122
ChainResidueDetails
AGLY72
BALA231
BLYS251
BGLY319
BLYS326
BALA348
ALEU115
AALA231
ALYS251
AGLY319
ALYS326
AALA348
BGLY72
BLEU115

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 52
ChainResidueDetails
AHIS110hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
ACYS111metal ligand
AASP183hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AGLY227metal ligand
AGLY265metal ligand
AILE287electrostatic stabiliser, hydrogen bond donor, steric role

site_idMCSA2
Number of Residues6
DetailsM-CSA 52
ChainResidueDetails
BHIS110hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BCYS111metal ligand
BASP183hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BGLY227metal ligand
BGLY265metal ligand
BILE287electrostatic stabiliser, hydrogen bond donor, steric role

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PDB entries from 2024-04-24

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