<?xml version="1.0" encoding="UTF-8"?>
<entry>
	<accession>MF7000233</accession>
	<general>
		<name>DR2232 (E46A mutant)</name>
		<pdb_id>5hwu</pdb_id>
		<exp_method>X-ray</exp_method>
		<resolution>2.10</resolution>
		<assembly>Homodimer</assembly>
		<source_organism>Deinococcus radiodurans</source_organism>
		<publication>
			<pmid>27739259</pmid>
			<authors>Mota CS, Gonçalves AM, de Sanctis D</authors>
			<title>Deinococcus radiodurans DR2231 is a two-metal-ion mechanism hydrolase with exclusive activity on dUTP.</title>
			<journal>FEBS J.</journal>
			<year>2016</year>
			<issue>23</issue>
			<volume>283</volume>
			<pages>4274-4290</pages>
		</publication>
	</general>
	<function>
		<molecular_function>
			<go>
				<accession>GO:0046872</accession>
				<name>metal ion binding</name>
			</go>
			<go>
				<accession>GO:0047429</accession>
				<name>nucleoside triphosphate diphosphatase activity</name>
			</go>
		</molecular_function>
	</function>
	<macromolecules>
		<general>
			<nr_of_chains>2</nr_of_chains>
			<nr_of_unique_protein_segments>1</nr_of_unique_protein_segments>
			<class>Homooligomeric enzymes</class>
			<subclass>Homodimeric enzymes</subclass>
			<note>All chains according to the most probable oligomerization state stored in PDBe were considered.</note>
		</general>
		<chain>
			<id>A</id>
			<name>HAD superfamily Cof-like phosphohydrolase</name>
			<source_organism>Deinococcus radiodurans</source_organism>
			<uniprot>
				<id>Q9RS96</id>
				<start>7</start>
				<end>144</end>
				<coverage>93%</coverage>
				<sequence>MSDLPCPPTNAERLHEFHRAIGAATPERPTPPPPELLRLRQTLLDEESAEVRAEIDHLLARQAAGEALSAGDLAPLAHELADLLYVTYGALDQLGIDADAVFAEVHRANLSKASGPRRADGKQLKPEGWRPADVRGVIERLQHAPADD</sequence>
				<length>148</length>
			</uniprot>
			<regions>
				<region>
					<region_type>secondary structure</region_type>
					<region_name>helix</region_name>
					<region_start>3</region_start>
					<region_end>15</region_end>
				</region>
				<region>
					<region_type>secondary structure</region_type>
					<region_name>helix</region_name>
					<region_start>27</region_start>
					<region_end>58</region_end>
				</region>
				<region>
					<region_type>secondary structure</region_type>
					<region_name>helix</region_name>
					<region_start>64</region_start>
					<region_end>66</region_end>
				</region>
				<region>
					<region_type>secondary structure</region_type>
					<region_name>helix</region_name>
					<region_start>67</region_start>
					<region_end>88</region_end>
				</region>
				<region>
					<region_type>secondary structure</region_type>
					<region_name>helix</region_name>
					<region_start>91</region_start>
					<region_end>105</region_end>
				</region>
				<region>
					<region_type>secondary structure</region_type>
					<region_name>helix</region_name>
					<region_start>127</region_start>
					<region_end>137</region_end>
				</region>
				<region>
					<region_type>pfam</region_type>
					<region_id>PF01503</region_id>
					<region_name>Phosphoribosyl-ATP pyrophosphohydrolase</region_name>
					<region_start>14</region_start>
					<region_end>109</region_end>
				</region>
			</regions>
		</chain>
		<chain>
			<id>B</id>
			<name>HAD superfamily Cof-like phosphohydrolase</name>
			<source_organism>Deinococcus radiodurans</source_organism>
			<uniprot>
				<id>Q9RS96</id>
				<start>7</start>
				<end>144</end>
				<coverage>93%</coverage>
				<sequence>MSDLPCPPTNAERLHEFHRAIGAATPERPTPPPPELLRLRQTLLDEESAEVRAEIDHLLARQAAGEALSAGDLAPLAHELADLLYVTYGALDQLGIDADAVFAEVHRANLSKASGPRRADGKQLKPEGWRPADVRGVIERLQHAPADD</sequence>
				<length>148</length>
			</uniprot>
			<regions>
				<region>
					<region_type>secondary structure</region_type>
					<region_name>helix</region_name>
					<region_start>3</region_start>
					<region_end>15</region_end>
				</region>
				<region>
					<region_type>secondary structure</region_type>
					<region_name>helix</region_name>
					<region_start>27</region_start>
					<region_end>58</region_end>
				</region>
				<region>
					<region_type>secondary structure</region_type>
					<region_name>helix</region_name>
					<region_start>64</region_start>
					<region_end>66</region_end>
				</region>
				<region>
					<region_type>secondary structure</region_type>
					<region_name>helix</region_name>
					<region_start>67</region_start>
					<region_end>88</region_end>
				</region>
				<region>
					<region_type>secondary structure</region_type>
					<region_name>helix</region_name>
					<region_start>91</region_start>
					<region_end>107</region_end>
				</region>
				<region>
					<region_type>secondary structure</region_type>
					<region_name>helix</region_name>
					<region_start>127</region_start>
					<region_end>137</region_end>
				</region>
				<region>
					<region_type>pfam</region_type>
					<region_id>PF01503</region_id>
					<region_name>Phosphoribosyl-ATP pyrophosphohydrolase</region_name>
					<region_start>14</region_start>
					<region_end>109</region_end>
				</region>
			</regions>
		</chain>
	</macromolecules>
	<evidence>
		<evidence_level>Direct evidence</evidence_level>
		<evidence_coverage>The full structure participates in mutual synergistic folding.</evidence_coverage>
		<sequence_domain>Phosphoribosyl-ATP pyrophosphohydrolase</sequence_domain>
		<complex_evidence>Phosphoribosyl-ATP pyrophosphohydrolases show a very unusual interlaced segment-swapped dimer, which implies that this obligatory dimer assembly is important for their function. Size-exclusion chromatography combined with static light scattering confirmed that the dimer is the major oligomeric state in solution (PMID:20944217). Upon dimer formation, DR2231 helices 2 and 3 from one monomer stack antiparallel to helices 2′ and 3′ of the other monomer, respectively. A stable four-helix bundle is formed in the center. The intertwining of the two hairpin structures produces an extensive subunit-subunit interface (PMID:21733847).</complex_evidence>
		<chain_evidence>
			<chain_id>A</chain_id>
			<support>N/A</support>
		</chain_evidence>
		<chain_evidence>
			<chain_id>B</chain_id>
			<support>N/A</support>
		</chain_evidence>
	</evidence>
	<related_structures>
		<id>MF7000284</id>
		<id>MF7000232</id>
		<id>MF7000233</id>
	</related_structures>
</entry>
