4PV5
Crystal structure of mouse glyoxalase I in complexed with 18-beta-glycyrrhetinic acid
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004462 | molecular_function | lactoylglutathione lyase activity |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006357 | biological_process | regulation of transcription by RNA polymerase II |
| A | 0006749 | biological_process | glutathione metabolic process |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0009438 | biological_process | methylglyoxal metabolic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0019243 | biological_process | methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione |
| A | 0030316 | biological_process | osteoclast differentiation |
| A | 0043066 | biological_process | negative regulation of apoptotic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004462 | molecular_function | lactoylglutathione lyase activity |
| B | 0005654 | cellular_component | nucleoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006357 | biological_process | regulation of transcription by RNA polymerase II |
| B | 0006749 | biological_process | glutathione metabolic process |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0009438 | biological_process | methylglyoxal metabolic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0019243 | biological_process | methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione |
| B | 0030316 | biological_process | osteoclast differentiation |
| B | 0043066 | biological_process | negative regulation of apoptotic process |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 201 |
| Chain | Residue |
| A | GLN34 |
| A | GLU100 |
| A | HOH341 |
| B | HIS127 |
| B | GLU173 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CBW A 202 |
| Chain | Residue |
| B | ASN104 |
| A | ARG123 |
| A | LYS151 |
| A | GLY156 |
| B | ARG38 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 201 |
| Chain | Residue |
| A | HIS127 |
| A | GLU173 |
| A | HOH330 |
| B | GLN34 |
| B | GLU100 |
Functional Information from PROSITE/UniProt
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 | GLU173 | |
| B | GLU173 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18695250, ECO:0007744|PDB:4OPN |
| Chain | Residue | Details |
| A | GLN34 | |
| A | GLU100 | |
| B | GLN34 | |
| B | GLU100 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0007744|PDB:4KYH, ECO:0007744|PDB:4OPN |
| Chain | Residue | Details |
| A | ARG38 | |
| A | ASN104 | |
| B | ARG38 | |
| B | ASN104 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: in other chain => ECO:0007744|PDB:4OPN |
| Chain | Residue | Details |
| A | ARG123 | |
| A | LYS157 | |
| B | ARG123 | |
| B | LYS157 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | BINDING: in other chain => ECO:0000269|PubMed:18695250, ECO:0007744|PDB:4OPN |
| Chain | Residue | Details |
| A | HIS127 | |
| A | GLU173 | |
| B | HIS127 | |
| B | GLU173 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: N-acetylalanine => ECO:0000250|UniProtKB:Q04760 |
| Chain | Residue | Details |
| A | ALA2 | |
| B | ALA2 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-succinyllysine => ECO:0007744|PubMed:23806337 |
| Chain | Residue | Details |
| A | LYS88 | |
| B | LYS88 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q04760 |
| Chain | Residue | Details |
| A | THR107 | |
| B | THR107 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | MOD_RES: S-glutathionyl cysteine => ECO:0000250 |
| Chain | Residue | Details |
| A | CYS139 | |
| B | CYS139 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0007744|PubMed:23806337 |
| Chain | Residue | Details |
| A | LYS148 | |
| B | LYS148 |
