5GHJ

Crystal structure of human MTH1(G2K mutant) in complex with 2-oxo-dATP

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	29
Details	binding site for residue 6U4 A 201

Chain	Residue
A	TYR7
A	TRP117
A	ASP119
A	ASP120
A	TRP123
A	NA202
A	NA203
A	HOH309
A	HOH316
A	HOH318
A	HOH319
A	THR8
A	HOH322
A	HOH367
A	HOH370
A	HOH371
A	HOH374
A	HOH378
A	HOH397
A	HOH416
A	HOH447
B	HOH447
A	LEU9
A	ASN33
A	GLY36
A	GLY37
A	LYS38
A	PHE72
A	MET81

---

site_id	AC2
Number of Residues	6
Details	binding site for residue NA A 202

Chain	Residue
A	GLU52
A	6U4201
A	HOH309
A	HOH322
A	HOH366
A	HOH383

---

site_id	AC3
Number of Residues	6
Details	binding site for residue NA A 203

Chain	Residue
A	GLY36
A	GLU56
A	6U4201
A	HOH367
A	HOH378
A	HOH382

---

site_id	AC4
Number of Residues	19
Details	binding site for residue 6U4 B 201

Chain	Residue
B	TYR7
B	THR8
B	LEU9
B	LYS23
B	ASN33
B	GLY36
B	GLY37
B	LYS38
B	PHE72
B	MET81
B	TRP117
B	ASP119
B	ASP120
B	TRP123
B	NA202
B	HOH305
B	HOH330
B	HOH409
B	HOH418

---

site_id	AC5
Number of Residues	4
Details	binding site for residue NA B 202

Chain	Residue
B	GLY36
B	GLU56
B	6U4201
B	HOH342

---

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	258
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	42
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	12
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	2
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	6
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	10
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q7ZWC3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---