5AYR
The crystal structure of SAUGI/human UDG complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004844 | molecular_function | uracil DNA N-glycosylase activity |
| A | 0006281 | biological_process | DNA repair |
| A | 0006284 | biological_process | base-excision repair |
| A | 0016799 | molecular_function | hydrolase activity, hydrolyzing N-glycosyl compounds |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0004844 | molecular_function | uracil DNA N-glycosylase activity |
| C | 0006281 | biological_process | DNA repair |
| C | 0006284 | biological_process | base-excision repair |
| C | 0016799 | molecular_function | hydrolase activity, hydrolyzing N-glycosyl compounds |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 900 |
| Chain | Residue |
| A | ASP145 |
| A | ASN215 |
| A | HOH1006 |
| A | HOH1009 |
| A | HOH1071 |
| B | HOH1008 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 900 |
| Chain | Residue |
| B | HOH1027 |
| D | ASP88 |
| D | MG900 |
| B | ASP88 |
| B | MET89 |
| B | HOH1015 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue MG C 900 |
| Chain | Residue |
| C | ASP145 |
| C | ASN215 |
| C | HOH1007 |
| C | HOH1009 |
| C | HOH1029 |
| C | HOH1071 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue MG D 900 |
| Chain | Residue |
| B | ASP88 |
| B | MG900 |
| B | HOH1015 |
| D | ASP88 |
| D | MET89 |
| D | HOH1007 |
Functional Information from PROSITE/UniProt
| site_id | PS00130 |
| Number of Residues | 10 |
| Details | U_DNA_GLYCOSYLASE Uracil-DNA glycosylase signature. KVVIlGQDPY |
| Chain | Residue | Details |
| A | LYS138-TYR147 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_03166","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"9724657","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1SSP","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"8900285","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9724657","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1SSP","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"4SKN","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"8900285","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4SKN","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
