1RRS

MutY adenine glycosylase in complex with DNA containing an abasic site

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000701	molecular_function	purine-specific mismatch base pair DNA N-glycosylase activity
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	0006298	biological_process	mismatch repair
A	0006950	biological_process	response to stress
A	0006974	biological_process	DNA damage response
A	0016787	molecular_function	hydrolase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0019104	molecular_function	DNA N-glycosylase activity
A	0032357	molecular_function	oxidized purine DNA binding
A	0034039	molecular_function	8-oxo-7,8-dihydroguanine DNA N-glycosylase activity
A	0035485	molecular_function	adenine/guanine mispair binding
A	0046872	molecular_function	metal ion binding
A	0051536	molecular_function	iron-sulfur cluster binding
A	0051539	molecular_function	4 iron, 4 sulfur cluster binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA A 367

Chain	Residue
A	SER118
A	VAL123
A	HOH411
A	HOH412
A	HOH414

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site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SF4 A 400

Chain	Residue
A	CYS208
A	CYS214
A	ALA222
A	ARG153
A	LEU154
A	CYS198
A	CYS205

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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

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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

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site_id	SWS_FT_FI3
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"19841264","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"14961129","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19841264","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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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

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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

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1mud

Chain	Residue	Details
A	GLU43
A	ASN144

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site_id	MCSA1
Number of Residues	3
Details	M-CSA 807

Chain

Residue

Details

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