6TC6

Crystal structure of MutM from Neisseria meningitidis

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003676	molecular_function	nucleic acid binding
A	0003677	molecular_function	DNA binding
A	0003684	molecular_function	damaged DNA binding
A	0003906	molecular_function	DNA-(apurinic or apyrimidinic site) endonuclease activity
A	0006281	biological_process	DNA repair
A	0006284	biological_process	base-excision repair
A	0008270	molecular_function	zinc ion binding
A	0008534	molecular_function	oxidized purine nucleobase lesion DNA N-glycosylase activity
A	0016787	molecular_function	hydrolase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0016799	molecular_function	hydrolase activity, hydrolyzing N-glycosyl compounds
A	0016829	molecular_function	lyase activity
A	0019104	molecular_function	DNA N-glycosylase activity
A	0046872	molecular_function	metal ion binding
A	0140078	molecular_function	class I DNA-(apurinic or apyrimidinic site) endonuclease activity
C	0003676	molecular_function	nucleic acid binding
C	0003677	molecular_function	DNA binding
C	0003684	molecular_function	damaged DNA binding
C	0003906	molecular_function	DNA-(apurinic or apyrimidinic site) endonuclease activity
C	0006281	biological_process	DNA repair
C	0006284	biological_process	base-excision repair
C	0008270	molecular_function	zinc ion binding
C	0008534	molecular_function	oxidized purine nucleobase lesion DNA N-glycosylase activity
C	0016787	molecular_function	hydrolase activity
C	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
C	0016799	molecular_function	hydrolase activity, hydrolyzing N-glycosyl compounds
C	0016829	molecular_function	lyase activity
C	0019104	molecular_function	DNA N-glycosylase activity
C	0046872	molecular_function	metal ion binding
C	0140078	molecular_function	class I DNA-(apurinic or apyrimidinic site) endonuclease activity

Functional Information from PROSITE/UniProt

site_id	PS01242
Number of Residues	25
Details	ZF_FPG_1 Zinc finger FPG-type signature. Cpr..CGglVvketlgq....RGtfYCpnCQ

Chain	Residue	Details
A	CYS250-GLN274

---