Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004462 | molecular_function | lactoylglutathione lyase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0009636 | biological_process | response to toxic substance |
| A | 0016151 | molecular_function | nickel cation binding |
| A | 0016829 | molecular_function | lyase activity |
| A | 0019243 | biological_process | methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004462 | molecular_function | lactoylglutathione lyase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0009636 | biological_process | response to toxic substance |
| B | 0016151 | molecular_function | nickel cation binding |
| B | 0016829 | molecular_function | lyase activity |
| B | 0019243 | biological_process | methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NI A 1200 |
| Chain | Residue |
| A | HIS5 |
| A | GLU56 |
| B | HIS74 |
| B | GLU122 |
| B | HOH140 |
| B | HOH152 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NI A 1201 |
| Chain | Residue |
| B | HIS5 |
| B | GLU56 |
| B | HOH142 |
| A | HIS74 |
| A | GLU122 |
| A | HOH1213 |
Functional Information from PROSITE/UniProt
| site_id | PS00934 |
| Number of Residues | 22 |
| Details | GLYOXALASE_I_1 Glyoxalase I signature 1. HTmLrVgdlqRSidFYtkvLGM |
| Chain | Residue | Details |
| A | HIS5-MET26 | |
| site_id | PS00935 |
| Number of Residues | 13 |
| Details | GLYOXALASE_I_2 Glyoxalase I signature 2. GT.....AYGHIAlSvdN |
| Chain | Residue | Details |
| A | GLY69-ASN81 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000250 |
| Chain | Residue | Details |
| A | GLU122 | |
| B | GLU122 | |
| Chain | Residue | Details |
| A | HIS5 | |
| A | GLU56 | |
| B | HIS5 | |
| B | GLU56 | |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | ARG9 | |
| A | ASN60 | |
| B | ARG9 | |
| B | ASN60 | |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: in other chain => ECO:0000250 |
| Chain | Residue | Details |
| A | HIS74 | |
| B | HIS74 | |
| Chain | Residue | Details |
| A | GLU122 | |
| B | GLU122 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1fro |
| Chain | Residue | Details |
| A | GLU122 | |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1fro |
| Chain | Residue | Details |
| B | GLU122 | |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 359 |
| Chain | Residue | Details |
| A | HIS5 | metal ligand |
| A | GLU56 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
| A | HIS74 | metal ligand |
| A | GLU122 | hydrogen bond acceptor, metal ligand, proton acceptor, proton donor, proton relay |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 359 |
| Chain | Residue | Details |
| B | HIS5 | metal ligand |
| B | GLU56 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
| B | HIS74 | metal ligand |
| B | GLU122 | hydrogen bond acceptor, metal ligand, proton acceptor, proton donor, proton relay |
