7E44

Crystal structure of NudC complexed with dpCoA

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000210	molecular_function	NAD+ diphosphatase activity
A	0000287	molecular_function	magnesium ion binding
A	0006402	biological_process	mRNA catabolic process
A	0006742	biological_process	NADP+ catabolic process
A	0008270	molecular_function	zinc ion binding
A	0016787	molecular_function	hydrolase activity
A	0019677	biological_process	NAD+ catabolic process
A	0030145	molecular_function	manganese ion binding
A	0035529	molecular_function	NADH pyrophosphatase activity
A	0042803	molecular_function	protein homodimerization activity
A	0046872	molecular_function	metal ion binding
A	0048255	biological_process	mRNA stabilization
A	0110153	molecular_function	RNA NAD-cap (NMN-forming) hydrolase activity
A	0110155	biological_process	NAD-cap decapping
B	0000210	molecular_function	NAD+ diphosphatase activity
B	0000287	molecular_function	magnesium ion binding
B	0006402	biological_process	mRNA catabolic process
B	0006742	biological_process	NADP+ catabolic process
B	0008270	molecular_function	zinc ion binding
B	0016787	molecular_function	hydrolase activity
B	0019677	biological_process	NAD+ catabolic process
B	0030145	molecular_function	manganese ion binding
B	0035529	molecular_function	NADH pyrophosphatase activity
B	0042803	molecular_function	protein homodimerization activity
B	0046872	molecular_function	metal ion binding
B	0048255	biological_process	mRNA stabilization
B	0110153	molecular_function	RNA NAD-cap (NMN-forming) hydrolase activity
B	0110155	biological_process	NAD-cap decapping
E	0000210	molecular_function	NAD+ diphosphatase activity
E	0000287	molecular_function	magnesium ion binding
E	0006402	biological_process	mRNA catabolic process
E	0006742	biological_process	NADP+ catabolic process
E	0008270	molecular_function	zinc ion binding
E	0016787	molecular_function	hydrolase activity
E	0019677	biological_process	NAD+ catabolic process
E	0030145	molecular_function	manganese ion binding
E	0035529	molecular_function	NADH pyrophosphatase activity
E	0042803	molecular_function	protein homodimerization activity
E	0046872	molecular_function	metal ion binding
E	0048255	biological_process	mRNA stabilization
E	0110153	molecular_function	RNA NAD-cap (NMN-forming) hydrolase activity
E	0110155	biological_process	NAD-cap decapping
F	0000210	molecular_function	NAD+ diphosphatase activity
F	0000287	molecular_function	magnesium ion binding
F	0006402	biological_process	mRNA catabolic process
F	0006742	biological_process	NADP+ catabolic process
F	0008270	molecular_function	zinc ion binding
F	0016787	molecular_function	hydrolase activity
F	0019677	biological_process	NAD+ catabolic process
F	0030145	molecular_function	manganese ion binding
F	0035529	molecular_function	NADH pyrophosphatase activity
F	0042803	molecular_function	protein homodimerization activity
F	0046872	molecular_function	metal ion binding
F	0048255	biological_process	mRNA stabilization
F	0110153	molecular_function	RNA NAD-cap (NMN-forming) hydrolase activity
F	0110155	biological_process	NAD-cap decapping

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	492
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	84
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	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"27428510","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5IW4","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"27428510","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5IW5","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PubMed","id":"27428510","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27561816","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of NADH pyrophosphatase (1790429) from Escherichia coli K12 at 2.20 A resolution.","authoringGroup":["Joint center for structural genomics (JCSG)"]}},{"source":"PDB","id":"1VK6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2GB5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5ISY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5IW4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5IW5","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"27561816","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5ISY","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	36
Details	Binding site: {"evidences":[{"source":"PubMed","id":"27428510","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27561816","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5ISY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5IW4","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q9DCN1","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---