1VK6

Crystal structure of NADH pyrophosphatase (1790429) from Escherichia coli k12 at 2.20 A resolution

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	0006734	biological_process	obsolete NADH metabolic 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

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 301

Chain	Residue
A	CYS98
A	CYS101
A	CYS116
A	CYS119

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MPD A 302

Chain	Residue
A	ARG84
A	TRP112
A	PRO125
A	GLN198
A	HOH377

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MPD A 303

Chain	Residue
A	ASP2
A	LEU56
A	GLN58
A	HOH317
A	HOH367

---

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MPD A 304

Chain	Residue
A	CYS130
A	GLY159
A	TRP194
A	HOH388

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	GLY159-GLY180

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
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_FI2
Number of Residues	1
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_FI3
Number of Residues	4
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_FI4
Number of Residues	1
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_FI5
Number of Residues	8
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_FI6
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q9DCN1","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---