1P7M

SOLUTION STRUCTURE AND BASE PERTURBATION STUDIES REVEAL A NOVEL MODE OF ALKYLATED BASE RECOGNITION BY 3-METHYLADENINE DNA GLYCOSYLASE I

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0005515	molecular_function	protein binding
A	0006281	biological_process	DNA repair
A	0006284	biological_process	base-excision repair
A	0006307	biological_process	DNA alkylation repair
A	0008725	molecular_function	DNA-3-methyladenine glycosylase activity
A	0016787	molecular_function	hydrolase activity
A	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 188

Chain	Residue
A	CYS4
A	HIS17
A	HIS175
A	CYS179

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site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ADK A 189

Chain	Residue
A	TRP46
A	SER164
A	TRP6
A	TYR13
A	TYR16
A	TRP21
A	GLU38

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:12654914, ECO:0000269|PubMed:13129925, ECO:0007744|PDB:1NKU, ECO:0007744|PDB:1P7M

Chain	Residue	Details
A	CYS4
A	HIS17
A	HIS175
A	CYS179

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	a catalytic site defined by CSA, PubMed 13129925, 15102448

Chain	Residue	Details
A	GLU38
A	TRP46
A	TYR16

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site_id	MCSA1
Number of Residues	3
Details	M-CSA 655

Chain	Residue	Details
A	TYR16	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
A	GLU38	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
A	TRP46	electrostatic stabiliser, van der waals interaction

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