1FRO
HUMAN GLYOXALASE I WITH BENZYL-GLUTATHIONE INHIBITOR
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004462 | molecular_function | lactoylglutathione lyase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| 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 | 0030316 | biological_process | osteoclast differentiation |
| A | 0043066 | biological_process | negative regulation of apoptotic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0070062 | cellular_component | extracellular exosome |
| B | 0004462 | molecular_function | lactoylglutathione lyase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005654 | cellular_component | nucleoplasm |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| 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 | 0030316 | biological_process | osteoclast differentiation |
| B | 0043066 | biological_process | negative regulation of apoptotic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0070062 | cellular_component | extracellular exosome |
| C | 0004462 | molecular_function | lactoylglutathione lyase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005654 | cellular_component | nucleoplasm |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0005975 | biological_process | carbohydrate metabolic process |
| C | 0006357 | biological_process | regulation of transcription by RNA polymerase II |
| C | 0006749 | biological_process | glutathione metabolic process |
| C | 0008270 | molecular_function | zinc ion binding |
| C | 0009438 | biological_process | methylglyoxal metabolic process |
| C | 0016829 | molecular_function | lyase activity |
| C | 0030316 | biological_process | osteoclast differentiation |
| C | 0043066 | biological_process | negative regulation of apoptotic process |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0070062 | cellular_component | extracellular exosome |
| D | 0004462 | molecular_function | lactoylglutathione lyase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005654 | cellular_component | nucleoplasm |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0005975 | biological_process | carbohydrate metabolic process |
| D | 0006357 | biological_process | regulation of transcription by RNA polymerase II |
| D | 0006749 | biological_process | glutathione metabolic process |
| D | 0008270 | molecular_function | zinc ion binding |
| D | 0009438 | biological_process | methylglyoxal metabolic process |
| D | 0016829 | molecular_function | lyase activity |
| D | 0030316 | biological_process | osteoclast differentiation |
| D | 0043066 | biological_process | negative regulation of apoptotic process |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0070062 | cellular_component | extracellular exosome |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 201 |
| Chain | Residue |
| A | HIS126 |
| A | GLU172 |
| B | GLN33 |
| B | GLU99 |
| B | HOH202 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 201 |
| Chain | Residue |
| A | HOH202 |
| B | HIS126 |
| B | GLU172 |
| A | GLN33 |
| A | GLU99 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN C 201 |
| Chain | Residue |
| C | HIS126 |
| C | GLU172 |
| D | GLN33 |
| D | GLU99 |
| D | HOH254 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN D 201 |
| Chain | Residue |
| C | GLN33 |
| C | GLU99 |
| C | HOH202 |
| D | HIS126 |
| D | GLU172 |
| site_id | AC5 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE GSB A 200 |
| Chain | Residue |
| A | ARG122 |
| A | LYS150 |
| A | MET157 |
| A | PHE162 |
| A | GLU172 |
| A | MET183 |
| A | HOH213 |
| A | HOH227 |
| A | HOH246 |
| B | ARG37 |
| B | PHE62 |
| B | PHE67 |
| B | THR101 |
| B | ASN103 |
| B | HOH266 |
| C | SER17 |
| C | HOH264 |
| site_id | AC6 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE GSB B 200 |
| Chain | Residue |
| A | ARG37 |
| A | PHE62 |
| A | PHE67 |
| A | THR101 |
| A | ASN103 |
| A | HOH266 |
| B | ARG122 |
| B | LYS150 |
| B | MET157 |
| B | PHE162 |
| B | GLU172 |
| B | MET183 |
| B | HOH213 |
| B | HOH227 |
| D | ASP154 |
| D | LYS158 |
| D | HOH246 |
| site_id | AC7 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE GSB C 200 |
| Chain | Residue |
| A | HOH264 |
| C | ARG122 |
| C | LYS150 |
| C | MET157 |
| C | PHE162 |
| C | GLU172 |
| C | MET183 |
| C | HOH213 |
| C | HOH227 |
| C | HOH246 |
| D | ARG37 |
| D | PHE62 |
| D | PHE67 |
| D | THR101 |
| D | ASN103 |
| D | HOH316 |
| site_id | AC8 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE GSB D 200 |
| Chain | Residue |
| C | ARG37 |
| C | PHE62 |
| C | PHE67 |
| C | THR101 |
| C | ASN103 |
| C | HOH266 |
| D | ARG122 |
| D | LYS150 |
| D | MET157 |
| D | PHE162 |
| D | GLU172 |
| D | MET183 |
| D | HOH247 |
| D | HOH252 |
| D | HOH280 |
| D | HOH298 |
| site_id | GH1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR GSH MOIETY - SUBSTRATE BINDING SITE IS FORMED BY ZN2 HYD2 AND GSH2. |
| Chain | Residue |
| A | ARG37 |
| A | ASN103 |
| B | ARG122 |
| site_id | GH2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR GSH MOIETY - SUBSTRATE BINDING SITE IS FORMED BY ZN1 HYD1 AND GSH1. |
| Chain | Residue |
| B | ARG37 |
| B | ASN103 |
| A | ARG122 |
| site_id | GH3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR GSH MOIETY - SUBSTRATE BINDING SITE IS FORMED BY ZN2 HYD2 AND GSH2. |
| Chain | Residue |
| C | ARG37 |
| C | ASN103 |
| D | ARG122 |
| site_id | GH4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR GSH MOIETY - SUBSTRATE BINDING SITE IS FORMED BY ZN1 HYD1 AND GSH1. |
| Chain | Residue |
| D | ARG37 |
| D | ASN103 |
| C | ARG122 |
| site_id | HD2 |
| Number of Residues | 14 |
| Details | HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. |
| Chain | Residue |
| A | CYS60 |
| A | PHE62 |
| A | MET65 |
| A | PHE67 |
| A | LEU69 |
| A | PHE71 |
| A | ILE88 |
| A | LEU92 |
| B | MET157 |
| B | LEU160 |
| B | PHE162 |
| B | LEU174 |
| B | MET179 |
| B | MET183 |
| site_id | HD3 |
| Number of Residues | 14 |
| Details | HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. |
| Chain | Residue |
| B | CYS60 |
| B | PHE62 |
| B | MET65 |
| B | PHE67 |
| B | LEU69 |
| B | PHE71 |
| B | ILE88 |
| B | LEU92 |
| A | MET157 |
| A | LEU160 |
| A | PHE162 |
| A | LEU174 |
| A | MET179 |
| A | MET183 |
| site_id | HD4 |
| Number of Residues | 14 |
| Details | HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. |
| Chain | Residue |
| C | CYS60 |
| C | PHE62 |
| C | MET65 |
| C | PHE67 |
| C | LEU69 |
| C | PHE71 |
| C | ILE88 |
| C | LEU92 |
| D | MET157 |
| D | LEU160 |
| D | PHE162 |
| D | LEU174 |
| D | MET179 |
| D | MET183 |
| site_id | HD5 |
| Number of Residues | 14 |
| Details | HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. |
| Chain | Residue |
| D | CYS60 |
| D | PHE62 |
| D | MET65 |
| D | PHE67 |
| D | LEU69 |
| D | PHE71 |
| D | ILE88 |
| D | LEU92 |
| C | MET157 |
| C | LEU160 |
| C | PHE162 |
| C | LEU174 |
| C | MET179 |
| C | MET183 |
| site_id | ZN1 |
| Number of Residues | 6 |
| Details | ZINC BINDING SITE AT DIMER INTERFACE. |
| Chain | Residue |
| B | ZN201 |
| A | GLN33 |
| A | GLU99 |
| B | HIS126 |
| B | GLU172 |
| A | HOH202 |
| site_id | ZN2 |
| Number of Residues | 6 |
| Details | ZINC BINDING SITE AT DIMER INTERFACE. |
| Chain | Residue |
| A | HIS126 |
| A | GLU172 |
| B | HOH202 |
| A | ZN201 |
| B | GLN33 |
| B | GLU99 |
| site_id | ZN3 |
| Number of Residues | 6 |
| Details | ZINC BINDING SITE AT DIMER INTERFACE. |
| Chain | Residue |
| D | ZN201 |
| C | GLN33 |
| C | GLU99 |
| D | HIS126 |
| D | GLU172 |
| C | HOH202 |
| site_id | ZN4 |
| Number of Residues | 6 |
| Details | ZINC BINDING SITE AT DIMER INTERFACE. |
| Chain | Residue |
| C | ZN201 |
| D | GLN33 |
| D | GLU99 |
| C | HIS126 |
| C | GLU172 |
| D | HOH254 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:10521255, ECO:0000269|PubMed:9705294 |
| Chain | Residue | Details |
| A | GLU172 | |
| B | GLU172 | |
| C | GLU172 | |
| D | GLU172 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294 |
| Chain | Residue | Details |
| A | GLN33 | |
| A | GLU99 | |
| B | GLN33 | |
| B | GLU99 | |
| C | GLN33 | |
| C | GLU99 | |
| D | GLN33 | |
| D | GLU99 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ARG37 | |
| A | ASN103 | |
| B | ARG37 | |
| B | ASN103 | |
| C | ARG37 | |
| C | ASN103 | |
| D | ARG37 | |
| D | ASN103 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | BINDING: in other chain |
| Chain | Residue | Details |
| A | ARG122 | |
| A | LYS156 | |
| B | ARG122 | |
| B | LYS156 | |
| C | ARG122 | |
| C | LYS156 | |
| D | ARG122 | |
| D | LYS156 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | BINDING: in other chain => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294 |
| Chain | Residue | Details |
| A | HIS126 | |
| A | GLU172 | |
| B | HIS126 | |
| B | GLU172 | |
| C | HIS126 | |
| C | GLU172 | |
| D | HIS126 | |
| D | GLU172 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | MOD_RES: N-acetylalanine => ECO:0000269|PubMed:20454679, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:25944712 |
| Chain | Residue | Details |
| A | ALA1 | |
| B | ALA1 | |
| C | ALA1 | |
| D | ALA1 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9CPU0 |
| Chain | Residue | Details |
| A | LYS87 | |
| B | LYS87 | |
| C | LYS87 | |
| D | LYS87 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphothreonine => ECO:0000269|PubMed:19199007 |
| Chain | Residue | Details |
| A | THR106 | |
| B | THR106 | |
| C | THR106 | |
| D | THR106 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | MOD_RES: S-glutathionyl cysteine; alternate => ECO:0000269|PubMed:20454679 |
| Chain | Residue | Details |
| A | CYS138 | |
| B | CYS138 | |
| C | CYS138 | |
| D | CYS138 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9CPU0 |
| Chain | Residue | Details |
| A | LYS147 | |
| B | LYS147 | |
| C | LYS147 | |
| D | LYS147 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 10521255, 14641060, 11076566 |
| Chain | Residue | Details |
| A | GLU172 | |
| A | GLU99 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 32 |
| Chain | Residue | Details |
| A | GLN33 | metal ligand |
| A | GLU99 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
| A | HIS126 | metal ligand |
| A | GLU172 | hydrogen bond acceptor, metal ligand, proton acceptor, proton donor, proton relay |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 32 |
| Chain | Residue | Details |
| B | GLN33 | metal ligand |
| B | GLU99 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
| B | HIS126 | metal ligand |
| B | GLU172 | hydrogen bond acceptor, metal ligand, proton acceptor, proton donor, proton relay |
| site_id | MCSA3 |
| Number of Residues | 4 |
| Details | M-CSA 32 |
| Chain | Residue | Details |
| C | GLN33 | metal ligand |
| C | GLU99 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
| C | HIS126 | metal ligand |
| C | GLU172 | hydrogen bond acceptor, metal ligand, proton acceptor, proton donor, proton relay |
| site_id | MCSA4 |
| Number of Residues | 4 |
| Details | M-CSA 32 |
| Chain | Residue | Details |
| D | GLN33 | metal ligand |
| D | GLU99 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
| D | HIS126 | metal ligand |
| D | GLU172 | hydrogen bond acceptor, metal ligand, proton acceptor, proton donor, proton relay |
