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6BNN

Crystal structure of V278E-glyoxalase I mutant from Zea mays in space group P4(1)2(1)2

Functional Information from GO Data
ChainGOidnamespacecontents
A0004462molecular_functionlactoylglutathione lyase activity
A0005737cellular_componentcytoplasm
A0016829molecular_functionlyase 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 Residues8
Detailsbinding site for residue GSH A 301
ChainResidue
AARG120
AVAL125
ALYS126
AMET159
AARG161
ATYR191
AASN212
AFMT303

site_idAC2
Number of Residues6
Detailsbinding site for residue CO A 302
ChainResidue
AGLU144
AGLN157
AGLU208
AHOH497
AHOH532
AHIS96

site_idAC3
Number of Residues6
Detailsbinding site for residue FMT A 303
ChainResidue
AASN72
AARG161
AGSH301
AHOH454
AHOH467
AHOH496

site_idAC4
Number of Residues6
Detailsbinding site for residue FMT A 304
ChainResidue
ALYS49
AGLY69
APRO70
AASP89
AILE90
AGLY91

Functional Information from PROSITE/UniProt
site_idPS00934
Number of Residues22
DetailsGLYOXALASE_I_1 Glyoxalase I signature 1. QVmLrVgdleRSikFYekaLGM
ChainResidueDetails
AGLN157-MET178

site_idPS00935
Number of Residues13
DetailsGLYOXALASE_I_2 Glyoxalase I signature 2. GT.....GFGHFAiAndD
ChainResidueDetails
AGLY91-ASP103

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PDB entries from 2024-06-12

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