3RQ5

Crystal Structure of ADP/ATP-dependent NAD(P)H-hydrate dehydratase from Bacillus subtilis co-crystallized with ATP/Mg2+ and soaked with CoA

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	19
Details	BINDING SITE FOR RESIDUE COA A 277

Chain	Residue
A	TYR27
A	GLY215
A	ASP216
A	HOH308
A	HOH324
A	HOH352
A	HOH364
A	HOH366
A	HOH427
A	HOH428
A	HOH429
A	THR29
A	GLY56
A	LYS57
A	HIS149
A	ALA210
A	GLY212
A	GLY213
A	THR214

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site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 278

Chain	Residue
A	ASP37
A	PRO40
A	PRO68
A	ARG81
A	HOH325
A	HOH390

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site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A 279

Chain	Residue
A	TRP80
A	LEU92
A	GLU93
A	GLU94
A	TYR96

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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

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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	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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