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5KN8

MutY N-terminal domain in complex with undamaged DNA

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0003824molecular_functioncatalytic activity
A0006281biological_processDNA repair
A0006284biological_processbase-excision repair
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0019104molecular_functionDNA N-glycosylase activity
A0051539molecular_function4 iron, 4 sulfur cluster binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue SF4 A 301
ChainResidue
AARG153
ACYS198
ACYS205
ACYS208
ACYS214
AALA222

site_idAC2
Number of Residues6
Detailsbinding site for residue CA A 302
ChainResidue
AHOH499
AHOH507
DDA21
ASER118
AVAL123
AHOH415

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues28
DetailsDomain: {"description":"HhH","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"19841264","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19841264","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"14961129","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19841264","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsBinding 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"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"19841264","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"25995449","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 807
ChainResidueDetails
AGLU43activator, proton acceptor, proton donor
ATYR126electrostatic stabiliser
AASN144covalently attached, nucleofuge, nucleophile

239149

PDB entries from 2025-07-23

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