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1WAU

Structure of KDPG Aldolase E45N mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008675molecular_function2-dehydro-3-deoxy-phosphogluconate aldolase activity
A0008700molecular_function4-hydroxy-2-oxoglutarate aldolase activity
A0008948molecular_functionoxaloacetate decarboxylase activity
A0016020cellular_componentmembrane
A0016829molecular_functionlyase activity
A0016833molecular_functionoxo-acid-lyase activity
A0042802molecular_functionidentical protein binding
A0106009molecular_function(4S)-4-hydroxy-2-oxoglutarate aldolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A1214
ChainResidue
AGLY162
AGLY163
AILE164
ASER184
AHOH2098
AHOH2100
AHOH2101
AHOH2102

Functional Information from PROSITE/UniProt
site_idPS00160
Number of Residues14
DetailsALDOLASE_KDPG_KHG_2 KDPG and KHG aldolases Schiff-base forming residue. GlkeFKFFPAeanG
ChainResidueDetails
AGLY128-GLY141

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AASN45

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE:
ChainResidueDetails
AARG49

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE: Schiff-base intermediate with substrate
ChainResidueDetails
ALYS133

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING:
ChainResidueDetails
AALA8

site_idSWS_FT_FI5
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:16403639
ChainResidueDetails
ATHR73
ATHR161
AGLY163
ASER184
AARG49

site_idSWS_FT_FI6
Number of Residues1
DetailsBINDING: covalent => ECO:0000269|PubMed:16403639
ChainResidueDetails
ALYS133

site_idSWS_FT_FI7
Number of Residues1
DetailsSITE: Plays a major role in determining the stereoselectivity
ChainResidueDetails
ATHR161

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 550
ChainResidueDetails
AASN45proton acceptor, proton donor
AARG49electrostatic stabiliser, modifies pKa
ALYS133electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor

221051

PDB entries from 2024-06-12

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