8TJG
Structure of Nei2 from Mycobacterium smegmatis in complex with Zn2+
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000703 | molecular_function | oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity |
| A | 0003676 | molecular_function | nucleic acid binding |
| A | 0003677 | molecular_function | DNA binding |
| A | 0003684 | molecular_function | damaged DNA binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0003906 | molecular_function | DNA-(apurinic or apyrimidinic site) endonuclease activity |
| A | 0006281 | biological_process | DNA repair |
| A | 0006284 | biological_process | base-excision repair |
| A | 0006974 | biological_process | DNA damage response |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0016799 | molecular_function | hydrolase activity, hydrolyzing N-glycosyl compounds |
| A | 0016829 | molecular_function | lyase activity |
| A | 0019104 | molecular_function | DNA N-glycosylase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0140078 | molecular_function | class I DNA-(apurinic or apyrimidinic site) endonuclease activity |
Functional Information from PROSITE/UniProt
| site_id | PS01242 |
| Number of Residues | 25 |
| Details | ZF_FPG_1 Zinc finger FPG-type signature. Crr..CGtlIqtdrgge....RVtyWCpvCQ |
| Chain | Residue | Details |
| A | CYS225-GLN249 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 34 |
| Details | Zinc finger: {"description":"FPG-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00391","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Schiff-base intermediate with DNA","evidences":[{"source":"PROSITE-ProRule","id":"PRU00392","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"36610794","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"39012146","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00392","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor (in beta-elimination)","evidences":[{"source":"PROSITE-ProRule","id":"PRU00392","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"39012146","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8TJG","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
