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1GYN

Class II fructose 1,6-bisphosphate aldolase with Cadmium (not Zinc) in the active site

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
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CD A 401
ChainResidue
AHIS110
AHIS264
AHOH2055
AHOH2059
AHOH2060
AHOH2120

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CD A 402
ChainResidue
AHOH2079
AHOH2080
AASP144
ASER146
AGLU174

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CD A 403
ChainResidue
AHIS91
AHIS129
AHOH2043
AHOH2045
AHOH2046

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CD A 404
ChainResidue
ASER1
AASN27
AGLU246
AHIS256

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CD A 405
ChainResidue
AHIS252
AHOH2039
AHOH2098

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 Residues1
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:10080900
ChainResidueDetails
AHIS110

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
AASN62

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:10080900, ECO:0000269|PubMed:8836102, ECO:0000269|PubMed:8939754
ChainResidueDetails
ACYS111
ALEU145
ALEU175
AGLY227
AGLY265

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING:
ChainResidueDetails
AVAL228
AGLY266
AILE287

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:21151122
ChainResidueDetails
APRO9

site_idSWS_FT_FI6
Number of Residues7
DetailsMOD_RES: N6-succinyllysine => ECO:0000269|PubMed:21151122
ChainResidueDetails
AGLY72
ALEU115
APRO231
ALYS251
AGLY319
ALYS326
AALA348

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1b57
ChainResidueDetails
AASP109
AASN286

site_idMCSA1
Number of Residues4
DetailsM-CSA 52
ChainResidueDetails
AASP109hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AHIS110metal ligand
AHIS264metal ligand
AASN286electrostatic stabiliser, hydrogen bond donor, steric role

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PDB entries from 2025-07-02

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