5KN8
MutY N-terminal domain in complex with undamaged DNA
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003677 | molecular_function | DNA binding |
A | 0003824 | molecular_function | catalytic activity |
A | 0006281 | biological_process | DNA repair |
A | 0006284 | biological_process | base-excision repair |
A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
A | 0019104 | molecular_function | DNA N-glycosylase activity |
A | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | binding site for residue SF4 A 301 |
Chain | Residue |
A | ARG153 |
A | CYS198 |
A | CYS205 |
A | CYS208 |
A | CYS214 |
A | ALA222 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue CA A 302 |
Chain | Residue |
A | HOH499 |
A | HOH507 |
D | DA21 |
A | SER118 |
A | VAL123 |
A | HOH415 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 28 |
Details | Domain: {"description":"HhH","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"19841264","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"19841264","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"14961129","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19841264","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"14961129","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19841264","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25995449","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2009","submissionDatabase":"PDB data bank","title":"Structural illumination of a mutY glycosylase reaction coordinate intermediate.","authors":["O'Shea V.L.","Cao S.","Richards J.L.","Horvath M.P.","David S.S."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"SEP-2015","submissionDatabase":"PDB data bank","title":"Structure and stereochemistry of the base excision repair glycosylase MutY reveal a mechanism similar to retaining glycosidases.","authors":["Woods R.D.","O'Shea V.L.","Chu A.","Cao S.","Richards J.L.","Horvath M.P.","David S.S."]}},{"source":"PDB","id":"1RRQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1RRS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1VRL","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"19841264","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"25995449","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 3 |
Details | M-CSA 807 |
Chain | Residue | Details |
A | GLU43 | activator, proton acceptor, proton donor |
A | TYR126 | electrostatic stabiliser |
A | ASN144 | covalently attached, nucleofuge, nucleophile |