6VBH
Human XPG endonuclease catalytic domain
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003677 | molecular_function | DNA binding |
| A | 0003697 | molecular_function | single-stranded DNA binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004518 | molecular_function | nuclease activity |
| A | 0004519 | molecular_function | endonuclease activity |
| A | 0005634 | cellular_component | nucleus |
| A | 0006289 | biological_process | nucleotide-excision repair |
| A | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 1001 |
| Chain | Residue |
| A | ASP847 |
| A | ASN849 |
| A | LYS850 |
| A | HIS884 |
| A | GLY885 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 1002 |
| Chain | Residue |
| A | CYS871 |
| A | HOH1136 |
| A | GLN4 |
| A | GLY5 |
| A | LYS8 |
| A | GLY870 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 1003 |
| Chain | Residue |
| A | LYS952 |
| A | ARG970 |
| A | HOH1102 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 A 1004 |
| Chain | Residue |
| A | LEU83 |
| A | LYS85 |
| A | THR863 |
| A | GLU864 |
| A | HOH1128 |
| A | HOH1134 |
| A | HOH1152 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 1005 |
| Chain | Residue |
| A | ARG819 |
| A | TYR837 |
| A | HOH1122 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 1006 |
| Chain | Residue |
| A | TRP34 |
| A | GLN37 |
| A | HIS54 |
| A | THR57 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 1007 |
| Chain | Residue |
| A | TRP895 |
| A | ASP911 |
| A | ARG919 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 1008 |
| Chain | Residue |
| A | PRO867 |
| A | THR868 |
| A | VAL869 |
| A | HOH1110 |
| A | HOH1132 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 1009 |
| Chain | Residue |
| A | PRO782 |
| A | TYR783 |
| A | THR912 |
| A | HOH1143 |
| A | HOH1167 |
| site_id | AD1 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 A 1010 |
| Chain | Residue |
| A | ARG970 |
| A | HOH1150 |
| site_id | AD2 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 1011 |
| Chain | Residue |
| A | THR57 |
| A | HIS60 |
| A | HOH1141 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 1012 |
| Chain | Residue |
| A | LEU66 |
| A | TRP950 |
| A | GLY951 |
| A | HOH1176 |
| site_id | AD4 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 1013 |
| Chain | Residue |
| A | ARG94 |
| A | ARG98 |
| A | ARG126 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 1014 |
| Chain | Residue |
| A | ARG98 |
| A | ARG126 |
| A | GLY845 |
| A | HOH1130 |
| site_id | AD6 |
| Number of Residues | 1 |
| Details | binding site for residue SO4 A 1015 |
| Chain | Residue |
| A | ARG777 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00614","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P39748","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 95 |
| Details | Region: {"description":"I-domain","evidences":[{"source":"PubMed","id":"32522879","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 16 |
| Details | Region: {"description":"DNA-binding; may bind to the undamaged single-strand DNA of the DNA repair bubble","evidences":[{"source":"PubMed","id":"32821917","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6TUW","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"6TUX","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 32 |
| Details | Region: {"description":"DNA-binding; H2TH (helix-2turn-helix) motif which binds double-stranded DNA","evidences":[{"source":"PubMed","id":"32821917","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6TUW","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"6TUX","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | Region: {"description":"DNA-binding; may bind double-stranded DNA","evidences":[{"source":"PubMed","id":"32821917","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6TUW","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"6TUX","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
