3FZI

1.9 Angstrom structure of the thermophilic exonuclease III homologue Mth0212

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003677	molecular_function	DNA binding
A	0003824	molecular_function	catalytic activity
A	0003906	molecular_function	DNA-(apurinic or apyrimidinic site) endonuclease activity
A	0004518	molecular_function	nuclease activity
A	0004519	molecular_function	endonuclease activity
A	0006281	biological_process	DNA repair
A	0006284	biological_process	base-excision repair
A	0008081	molecular_function	phosphoric diester hydrolase activity
A	0008311	molecular_function	double-stranded DNA 3'-5' DNA exonuclease activity
A	0016787	molecular_function	hydrolase activity
A	0016829	molecular_function	lyase activity
A	0046872	molecular_function	metal ion binding
A	0140078	molecular_function	class I DNA-(apurinic or apyrimidinic site) endonuclease activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 266

Chain	Residue
A	ASN12
A	GLU38
A	LYS40
A	HOH334
A	HOH335
A	HOH391

---

Functional Information from PROSITE/UniProt

site_id	PS00726
Number of Residues	10
Details	AP_NUCLEASE_F1_1 AP endonucleases family 1 signature 1. PDILCLQEIK

Chain	Residue	Details
A	PRO31-LYS40

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:20434457

Chain	Residue	Details
A	ASP151

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:20434457, ECO:0000269|Ref.7

Chain	Residue	Details
A	ASN12
A	GLU38

---

site_id	SWS_FT_FI3
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:20434457

Chain	Residue	Details
A	ASP151
A	ASN153
A	HIS248

---