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2QED

Crystal structure of Salmonella thyphimurium LT2 glyoxalase II

Replaces:  2OBW
Functional Information from GO Data
ChainGOidnamespacecontents
A0004416molecular_functionhydroxyacylglutathione hydrolase activity
A0016787molecular_functionhydrolase activity
A0019243biological_processmethylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FE A 252
ChainResidue
AASP57
AHIS58
AASP127
AHIS165
AFE253
AHOH606
AHOH692

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FE A 253
ChainResidue
AHIS110
AASP127
AFE252
AHOH607
AHOH692
AHIS53
AHIS55

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO A 254
ChainResidue
APRO156
AASP157

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EDO A 255
ChainResidue
AGLN147

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO A 256
ChainResidue
ATYR146
ALEU149
AMET150
AASN153
APHE216
ALEU217
ATHR219
AHOH454

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 257
ChainResidue
AASN4
ASER5
AALA38
AGLU41
AHIS42

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 258
ChainResidue
AARG23
APRO46
AGLN71
AHOH582
AHOH722

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 259
ChainResidue
ALEU3
AASN4
ASER5
AMET201
AHOH294
AHOH296

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:17764159
ChainResidueDetails
AHIS53
AHIS55
AASP57
AHIS58
AHIS110
AASP127
AHIS165

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1qh5
ChainResidueDetails
AASP57

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PDB entries from 2024-07-17

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