4OPN
Crystal structure of mouse glyoxalase I complexed with mAH
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 | 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 | 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 |
| B | HIS127 |
| B | GLU173 |
| B | ZBF202 |
| site_id | AC2 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE ZBF A 202 |
| Chain | Residue |
| A | LYS157 |
| A | MET158 |
| A | LEU161 |
| A | PHE163 |
| A | GLU173 |
| A | ILE180 |
| A | HOH351 |
| A | HOH362 |
| A | HOH392 |
| B | GLN34 |
| B | ARG38 |
| B | PHE68 |
| B | LEU70 |
| B | GLU100 |
| B | THR102 |
| B | ASN104 |
| B | ZN201 |
| B | HOH347 |
| A | ARG123 |
| A | HIS127 |
| A | LYS151 |
| A | GLY156 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 201 |
| Chain | Residue |
| A | HIS127 |
| A | GLU173 |
| A | ZBF202 |
| B | GLN34 |
| B | GLU100 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE ZBF B 202 |
| Chain | Residue |
| A | GLN34 |
| A | ARG38 |
| A | PHE68 |
| A | LEU70 |
| A | PHE93 |
| A | GLU100 |
| A | THR102 |
| A | ASN104 |
| A | ZN201 |
| B | ARG123 |
| B | HIS127 |
| B | LYS151 |
| B | GLY156 |
| B | LYS157 |
| B | MET158 |
| B | PHE163 |
| B | GLU173 |
| B | LEU175 |
| B | HOH338 |
| B | HOH340 |
| B | HOH343 |
| B | HOH392 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 292 |
| Details | Domain: {"description":"VOC","evidences":[{"source":"PROSITE-ProRule","id":"PRU01163","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18695250","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4OPN","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"4KYH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4OPN","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"PDB","id":"4OPN","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"18695250","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4OPN","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"PubMed","id":"23806337","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q04760","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"S-glutathionyl cysteine","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"23806337","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
