1BH5
HUMAN GLYOXALASE I Q33E, E172Q DOUBLE MUTANT
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 | GLN172 |
B | GLU33 |
B | GLU99 |
B | HOH202 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN B 201 |
Chain | Residue |
A | GLU33 |
A | GLU99 |
A | HOH202 |
B | HIS126 |
B | GLN172 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN C 201 |
Chain | Residue |
C | HIS126 |
C | GLN172 |
C | HOH202 |
D | GLU33 |
D | GLU99 |
D | HOH203 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN D 201 |
Chain | Residue |
C | GLU33 |
C | GLU99 |
C | HOH203 |
C | HOH204 |
D | HIS126 |
D | GLN172 |
site_id | AC5 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE GTX A 200 |
Chain | Residue |
A | ARG122 |
A | MET157 |
A | PHE162 |
A | HOH275 |
A | HOH300 |
A | HOH315 |
A | HOH341 |
B | ARG37 |
B | CYS60 |
B | PHE67 |
B | LEU92 |
B | THR101 |
B | ASN103 |
C | SER17 |
C | HOH292 |
site_id | AC6 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE GTX B 200 |
Chain | Residue |
A | ARG37 |
A | CYS60 |
A | PHE67 |
A | THR101 |
A | ASN103 |
A | LYS139 |
A | HOH202 |
B | ARG122 |
B | LYS150 |
B | MET157 |
B | PHE162 |
B | MET183 |
B | HOH209 |
B | HOH213 |
B | HOH281 |
B | HOH328 |
site_id | AC7 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE GTX C 200 |
Chain | Residue |
A | SER17 |
C | ARG122 |
C | MET157 |
C | LEU160 |
C | PHE162 |
C | MET179 |
C | HOH210 |
C | HOH214 |
C | HOH278 |
C | HOH299 |
C | HOH306 |
C | HOH310 |
C | HOH314 |
D | ARG37 |
D | CYS60 |
D | PHE67 |
D | LEU92 |
D | ASN103 |
site_id | AC8 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE GTX D 200 |
Chain | Residue |
C | ARG37 |
C | CYS60 |
C | PHE67 |
C | THR101 |
C | ASN103 |
C | HOH245 |
D | ARG122 |
D | LEU160 |
D | PHE162 |
D | MET183 |
D | HOH280 |
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 | GLU33 |
A | GLU99 |
B | HIS126 |
B | GLN172 |
A | HOH202 |
site_id | ZN2 |
Number of Residues | 7 |
Details | ZINC BINDING SITE AT DIMER INTERFACE. |
Chain | Residue |
A | HIS126 |
A | GLN172 |
B | HOH202 |
B | HOH203 |
A | ZN201 |
B | GLU33 |
B | GLU99 |
site_id | ZN3 |
Number of Residues | 7 |
Details | ZINC BINDING SITE AT DIMER INTERFACE. |
Chain | Residue |
D | ZN201 |
C | GLU33 |
C | GLU99 |
D | HIS126 |
D | GLN172 |
C | HOH203 |
C | HOH204 |
site_id | ZN4 |
Number of Residues | 6 |
Details | ZINC BINDING SITE AT DIMER INTERFACE. |
Chain | Residue |
C | ZN201 |
D | GLU33 |
D | GLU99 |
C | HIS126 |
C | GLN172 |
C | HOH202 |
Functional Information from PROSITE/UniProt
site_id | PS00935 |
Number of Residues | 17 |
Details | GLYOXALASE_I_2 Glyoxalase I signature 2. GNsdpr.GFGHIGiAvpD |
Chain | Residue | Details |
A | GLY117-ASP133 |
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 |
B | ILE173 | |
C | ILE173 | |
D | ILE173 | |
A | ILE173 |
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 |
B | THR34 | |
B | LEU100 | |
C | THR34 | |
C | LEU100 | |
D | THR34 | |
D | LEU100 | |
A | THR34 | |
A | LEU100 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: |
Chain | Residue | Details |
C | VAL38 | |
C | TRP104 | |
D | VAL38 | |
D | TRP104 | |
A | VAL38 | |
A | TRP104 | |
B | VAL38 | |
B | TRP104 |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | BINDING: in other chain |
Chain | Residue | Details |
C | GLY123 | |
C | MET157 | |
D | GLY123 | |
D | MET157 | |
A | GLY123 | |
A | MET157 | |
B | GLY123 | |
B | MET157 |
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 | ILE127 | |
A | ILE173 | |
B | ILE127 | |
B | ILE173 | |
C | ILE127 | |
C | ILE173 | |
D | ILE127 | |
D | ILE173 |
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 | GLU2 | |
B | GLU2 | |
C | GLU2 | |
D | GLU2 |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9CPU0 |
Chain | Residue | Details |
A | ILE88 | |
B | ILE88 | |
C | ILE88 | |
D | ILE88 |
site_id | SWS_FT_FI8 |
Number of Residues | 4 |
Details | MOD_RES: Phosphothreonine => ECO:0000269|PubMed:19199007 |
Chain | Residue | Details |
A | GLU107 | |
B | GLU107 | |
C | GLU107 | |
D | GLU107 |
site_id | SWS_FT_FI9 |
Number of Residues | 4 |
Details | MOD_RES: S-glutathionyl cysteine; alternate => ECO:0000269|PubMed:20454679 |
Chain | Residue | Details |
A | LYS139 | |
B | LYS139 | |
C | LYS139 | |
D | LYS139 |
site_id | SWS_FT_FI10 |
Number of Residues | 4 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9CPU0 |
Chain | Residue | Details |
A | PHE148 | |
B | PHE148 | |
C | PHE148 | |
D | PHE148 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 32 |
Chain | Residue | Details |
A | THR34 | metal ligand |
A | LEU100 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
A | ILE127 | metal ligand |
A | ILE173 | 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 | THR34 | metal ligand |
B | LEU100 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
B | ILE127 | metal ligand |
B | ILE173 | 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 | THR34 | metal ligand |
C | LEU100 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
C | ILE127 | metal ligand |
C | ILE173 | 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 | THR34 | metal ligand |
D | LEU100 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
D | ILE127 | metal ligand |
D | ILE173 | hydrogen bond acceptor, metal ligand, proton acceptor, proton donor, proton relay |