3RQQ

Crystal Structure of ADP/ATP-dependent NAD(P)H-hydrate dehydratase from Bacillus subtilis in complex with P1,P3-Di(adenosine-5') triphosphate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0016836	molecular_function	hydro-lyase activity
A	0046496	biological_process	nicotinamide nucleotide metabolic process
A	0052855	molecular_function	ADP-dependent NAD(P)H-hydrate dehydratase activity
A	0052856	molecular_function	NAD(P)HX epimerase activity
A	0110051	biological_process	metabolite repair

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG A 277

Chain	Residue
A	LYS186
A	BA3278
A	HOH305
A	HOH308

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site_id	AC2
Number of Residues	24
Details	BINDING SITE FOR RESIDUE BA3 A 278

Chain	Residue
A	GLY187
A	THR190
A	ASN206
A	GLY207
A	LEU209
A	ALA210
A	GLY212
A	GLY213
A	THR214
A	GLY215
A	ASP216
A	LEU218
A	HIS243
A	MG277
A	HOH295
A	HOH305
A	HOH308
A	HOH341
A	HOH395
A	ALA20
A	SER22
A	LYS24
A	HIS149
A	LYS186

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Functional Information from PROSITE/UniProt

site_id	PS01049
Number of Residues	11
Details	YJEF_C_1 YjeF C-terminal domain signature 1. AIAIGPGLPqT

Chain	Residue	Details
A	ALA98-THR108

---

site_id	PS01050
Number of Residues	11
Details	YJEF_C_2 YjeF C-terminal domain signature 2. GGtGDTLTGmI

Chain	Residue	Details
A	GLY212-ILE222

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	268
Details	Domain: {"description":"YjeF C-terminal","evidences":[{"source":"HAMAP-Rule","id":"MF_01965","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	9
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22940582","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3RPZ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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