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6BNZ

Crystal structure of E144Q-glyoxalase I mutant from Zea mays in space group P4(1)2(1)2

Functional Information from GO Data
ChainGOidnamespacecontents
A0004462molecular_functionlactoylglutathione lyase activity
A0016829molecular_functionlyase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue CO A 301
ChainResidue
AHIS96
AGLN144
AGLN157
AGLU208
AHOH464
AHOH477

site_idAC2
Number of Residues10
Detailsbinding site for residue GSH A 302
ChainResidue
APHE134
AARG161
ATYR191
AASN212
AFMT304
AHOH411
AHOH565
AARG120
AVAL125
ALYS126

site_idAC3
Number of Residues7
Detailsbinding site for residue FMT A 303
ChainResidue
ALYS49
ALEU51
AGLY69
APRO70
AASP89
AILE90
AGLY91

site_idAC4
Number of Residues5
Detailsbinding site for residue FMT A 304
ChainResidue
AASN72
AARG161
AGSH302
AHOH431
AHOH476

site_idAC5
Number of Residues4
Detailsbinding site for residue FMT A 305
ChainResidue
AARG31
ATHR80
AFMT306
AHOH546

site_idAC6
Number of Residues5
Detailsbinding site for residue FMT A 306
ChainResidue
AARG31
AGLN226
ALYS276
AFMT305
AHOH418

site_idAC7
Number of Residues3
Detailsbinding site for residue FMT A 307
ChainResidue
AARG182
AARG182
ALYS184

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 2024-11-06

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