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6OVI

Crystal Structure of KDPG Aldolase from Legionella Pneumophila with pyruvate captured at low pH as a covalent carbinolamine intermediate

Functional Information from GO Data
ChainGOidnamespacecontents
A0008675molecular_function2-dehydro-3-deoxy-phosphogluconate aldolase activity
A0016829molecular_functionlyase activity
B0008675molecular_function2-dehydro-3-deoxy-phosphogluconate aldolase activity
B0016829molecular_functionlyase activity
C0008675molecular_function2-dehydro-3-deoxy-phosphogluconate aldolase activity
C0016829molecular_functionlyase activity
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue PVO A 301
ChainResidue
AGLU55
AARG59
ATHR83
AILE102
ASER103
APRO104
ALYS143
APHE145

site_idAC2
Number of Residues3
Detailsbinding site for residue EDO A 302
ChainResidue
AHOH403
AHOH436
AHIS141

site_idAC3
Number of Residues5
Detailsbinding site for residue SO4 A 303
ChainResidue
AGLY173
AGLY193
ASER194
AHOH411
AHOH422

site_idAC4
Number of Residues6
Detailsbinding site for residue SO4 A 304
ChainResidue
AARG108
AHOH402
AHOH431
AHOH482
BARG108
CARG108

site_idAC5
Number of Residues9
Detailsbinding site for residue SO4 A 305
ChainResidue
AALA149
AALA150
AGLY151
AHOH409
BALA149
BALA150
CALA149
CALA150
CGLY151

site_idAC6
Number of Residues4
Detailsbinding site for residue EDO B 302
ChainResidue
BTYR179
BGLU180
BLEU183
BVAL217

site_idAC7
Number of Residues6
Detailsbinding site for residue EDO B 303
ChainResidue
AGLU109
BARG108
BGLY136
BMET137
BHOH413
BHOH451

site_idAC8
Number of Residues7
Detailsbinding site for residue SO4 B 304
ChainResidue
BGLY173
BGLY193
BSER194
BHOH416
BHOH438
BHOH456
BHOH515

site_idAC9
Number of Residues3
Detailsbinding site for residue EDO C 302
ChainResidue
CGLY136
CHOH412
CHOH420

site_idAD1
Number of Residues7
Detailsbinding site for residue SO4 C 303
ChainResidue
CGLY173
CGLY193
CSER194
CHOH417
CHOH446
CHOH457
CHOH471

site_idAD2
Number of Residues8
Detailsbinding site for residue SO4 C 304
ChainResidue
AARG108
CTHR107
CARG108
CGLU109
CHOH411
CHOH413
CHOH433
CHOH448

Functional Information from PROSITE/UniProt
site_idPS00159
Number of Residues10
DetailsALDOLASE_KDPG_KHG_1 KDPG and KHG aldolases active site. GIhvlEVTLR
ChainResidueDetails
AGLY50-ARG59

site_idPS00160
Number of Residues14
DetailsALDOLASE_KDPG_KHG_2 KDPG and KHG aldolases Schiff-base forming residue. GynhFKFFPAaaaG
ChainResidueDetails
AGLY138-GLY151

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PDB entries from 2024-07-24

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