3N5N

Crystal structure analysis of the catalytic domain and interdomain connector of human MutY homologue

Functional Information from GO Data

Chain	GOid	namespace	contents
X	0003677	molecular_function	DNA binding
X	0003824	molecular_function	catalytic activity
X	0006281	biological_process	DNA repair
X	0006284	biological_process	base-excision repair
X	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
X	0051539	molecular_function	4 iron, 4 sulfur cluster binding
Y	0003677	molecular_function	DNA binding
Y	0003824	molecular_function	catalytic activity
Y	0006281	biological_process	DNA repair
Y	0006284	biological_process	base-excision repair
Y	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
Y	0051539	molecular_function	4 iron, 4 sulfur cluster binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SF4 X 400

Chain	Residue
X	CYS276
X	CYS283
X	CYS286
X	CYS292

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site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SF4 Y 400

Chain	Residue
Y	CYS292
Y	ARG231
Y	VAL232
Y	CYS276
Y	CYS283
Y	CYS286

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site_id	AC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE ACT Y 2

Chain	Residue
Y	GLY184

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Functional Information from PROSITE/UniProt

site_id	PS00764
Number of Residues	17
Details	ENDONUCLEASE_III_1 Endonuclease III iron-sulfur binding region signature. CtpqRPLCsqCpveslC

Chain	Residue	Details
X	CYS276-CYS292

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site_id	PS01155
Number of Residues	31
Details	ENDONUCLEASE_III_2 Endonuclease III family signature. GhMPrtaetLqqlLPGVGrytAgaiAsiAFG

Chain	Residue	Details
X	GLY185-GLY215

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:P83847

Chain	Residue	Details
X	GLU120
Y	GLU120

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site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
X	CYS276
X	CYS283
X	CYS286
X	CYS292
Y	CYS276
Y	CYS283
Y	CYS286
Y	CYS292

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site_id	SWS_FT_FI3
Number of Residues	2
Details	SITE: Transition state stabilizer => ECO:0000250|UniProtKB:P83847

Chain	Residue	Details
X	ASP222
Y	ASP222

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