5FSN

MTH1 substrate recognition: Complex with a aminomethylpyrimidinyl oxypropanol.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003723	molecular_function	RNA binding
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005759	cellular_component	mitochondrial matrix
A	0005829	cellular_component	cytosol
A	0006152	biological_process	purine nucleoside catabolic process
A	0006281	biological_process	DNA repair
A	0006979	biological_process	response to oxidative stress
A	0008413	molecular_function	8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity
A	0008828	molecular_function	dATP diphosphatase activity
A	0016787	molecular_function	hydrolase activity
A	0016818	molecular_function	hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
A	0030515	molecular_function	snoRNA binding
A	0035539	molecular_function	8-oxo-7,8-dihydrodeoxyguanosine triphosphate pyrophosphatase activity
A	0042262	biological_process	DNA protection
A	0046872	molecular_function	metal ion binding
A	0047693	molecular_function	ATP diphosphatase activity
A	0106377	molecular_function	2-hydroxy-ATP hydrolase activity
A	0106378	molecular_function	2-hydroxy-dATP hydrolase activity
A	0106431	molecular_function	N6-methyl-(d)ATP hydrolase activity
A	0106433	molecular_function	O6-methyl-dGTP hydrolase activity
A	0140933	molecular_function	5'-(N(7)-methylguanosine 5'-triphospho)-[mRNA] hydrolase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE 6Q3 A 201

Chain	Residue
A	THR8
A	ACT202
A	PHE27
A	GLY36
A	PHE72
A	MET81
A	TRP117
A	ASP119
A	ASP120
A	PHE139

---

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE ACT A 202

Chain	Residue
A	LEU9
A	ASN33
A	GLY34
A	ASP120
A	TRP123
A	PHE124
A	6Q3201
A	HOH321

---

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE DMS A 203

Chain	Residue
A	TYR148
A	LEU150

---

Functional Information from PROSITE/UniProt

site_id	PS00893
Number of Residues	22
Details	NUDIX_BOX Nudix box signature. GkvqegEtiedGArRELqEEsG

Chain	Residue	Details
A	GLY37-GLY58

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	129
Details	Domain: {"description":"Nudix hydrolase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00794","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	21
Details	Motif: {"description":"Nudix box","evidences":[{"source":"PROSITE-ProRule","id":"PRU00794","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"30304478","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5OTM","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"26999531","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5FSK","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"26999531","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28035004","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5FSI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5GHI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5GHM","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	5
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q7ZWC3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---