Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6C8Q

Crystal structure of NAD synthetase (NadE) from Enterococcus faecalis in complex with NAD+

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0003952	molecular_function	NAD+ synthase (glutamine-hydrolyzing) activity
A	0004359	molecular_function	glutaminase activity
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0008795	molecular_function	NAD+ synthase activity
A	0009435	biological_process	NAD biosynthetic process
A	0016874	molecular_function	ligase activity
A	0046872	molecular_function	metal ion binding
B	0000166	molecular_function	nucleotide binding
B	0003952	molecular_function	NAD+ synthase (glutamine-hydrolyzing) activity
B	0004359	molecular_function	glutaminase activity
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0008795	molecular_function	NAD+ synthase activity
B	0009435	biological_process	NAD biosynthetic process
B	0016874	molecular_function	ligase activity
B	0046872	molecular_function	metal ion binding
C	0000166	molecular_function	nucleotide binding
C	0003952	molecular_function	NAD+ synthase (glutamine-hydrolyzing) activity
C	0004359	molecular_function	glutaminase activity
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0008795	molecular_function	NAD+ synthase activity
C	0009435	biological_process	NAD biosynthetic process
C	0016874	molecular_function	ligase activity
C	0046872	molecular_function	metal ion binding
D	0000166	molecular_function	nucleotide binding
D	0003952	molecular_function	NAD+ synthase (glutamine-hydrolyzing) activity
D	0004359	molecular_function	glutaminase activity
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0008795	molecular_function	NAD+ synthase activity
D	0009435	biological_process	NAD biosynthetic process
D	0016874	molecular_function	ligase activity
D	0046872	molecular_function	metal ion binding
E	0000166	molecular_function	nucleotide binding
E	0003952	molecular_function	NAD+ synthase (glutamine-hydrolyzing) activity
E	0004359	molecular_function	glutaminase activity
E	0005524	molecular_function	ATP binding
E	0005737	cellular_component	cytoplasm
E	0008795	molecular_function	NAD+ synthase activity
E	0009435	biological_process	NAD biosynthetic process
E	0016874	molecular_function	ligase activity
E	0046872	molecular_function	metal ion binding
F	0000166	molecular_function	nucleotide binding
F	0003952	molecular_function	NAD+ synthase (glutamine-hydrolyzing) activity
F	0004359	molecular_function	glutaminase activity
F	0005524	molecular_function	ATP binding
F	0005737	cellular_component	cytoplasm
F	0008795	molecular_function	NAD+ synthase activity
F	0009435	biological_process	NAD biosynthetic process
F	0016874	molecular_function	ligase activity
F	0046872	molecular_function	metal ion binding
G	0000166	molecular_function	nucleotide binding
G	0003952	molecular_function	NAD+ synthase (glutamine-hydrolyzing) activity
G	0004359	molecular_function	glutaminase activity
G	0005524	molecular_function	ATP binding
G	0005737	cellular_component	cytoplasm
G	0008795	molecular_function	NAD+ synthase activity
G	0009435	biological_process	NAD biosynthetic process
G	0016874	molecular_function	ligase activity
G	0046872	molecular_function	metal ion binding
H	0000166	molecular_function	nucleotide binding
H	0003952	molecular_function	NAD+ synthase (glutamine-hydrolyzing) activity
H	0004359	molecular_function	glutaminase activity
H	0005524	molecular_function	ATP binding
H	0005737	cellular_component	cytoplasm
H	0008795	molecular_function	NAD+ synthase activity
H	0009435	biological_process	NAD biosynthetic process
H	0016874	molecular_function	ligase activity
H	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	21
Details	binding site for residue NAD A 301

Chain	Residue
A	PHE133
A	LYS262
A	HOH402
A	HOH455
A	HOH490
B	TYR34
B	HIS38
B	PHE40
B	TYR148
B	GLY156
B	ASP181
A	ASN137
C	VAL226
C	GLY229
A	ARG141
A	PHE171
A	PHE172
A	THR173
A	LYS174
A	ALA227
A	HIS261

site_id	AC2
Number of Residues	18
Details	binding site for residue NAD B 301

Chain	Residue
A	TYR34
A	HIS38
A	PHE40
A	TYR148
A	GLY156
A	ASP181
B	PHE133
B	ASN137
B	ARG141
B	ALA170
B	PHE171
B	PHE172
B	THR173
B	LYS174
B	ALA227
B	HIS261
B	LYS262
B	HOH472

site_id	AC3
Number of Residues	21
Details	binding site for residue NAD C 301

Chain	Residue
A	VAL226
A	GLY229
C	PHE133
C	ASN137
C	ARG141
C	ALA170
C	PHE171
C	PHE172
C	THR173
C	LYS174
C	ALA227
C	HIS261
C	LYS262
C	HOH401
C	HOH411
G	TYR34
G	HIS38
G	PHE40
G	TYR148
G	GLY156
G	ASP181

site_id	AC4
Number of Residues	15
Details	binding site for residue NAD D 301

Chain	Residue
D	PHE133
D	ASN137
D	ARG141
D	PHE171
D	PHE172
D	LYS174
D	HIS261
D	LYS262
D	HOH419
D	HOH462
F	TYR34
F	HIS38
F	PHE40
F	GLY156
F	ASP181

site_id	AC5
Number of Residues	16
Details	binding site for residue NAD E 301

Chain	Residue
E	PHE133
E	ASN137
E	ARG141
E	PHE171
E	PHE172
E	THR173
E	LYS174
E	HIS261
E	LYS262
E	HOH415
H	TYR34
H	HIS38
H	PHE40
H	GLY156
H	ALA157
H	ASP181

site_id	AC6
Number of Residues	16
Details	binding site for residue NAD F 301

Chain	Residue
F	ASN137
F	ARG141
F	PHE171
F	PHE172
F	THR173
F	LYS174
F	HIS261
F	LYS262
D	TYR34
D	HIS38
D	LEU41
D	TYR148
D	GLY156
D	ASP181
F	PHE133
F	GLY136

site_id	AC7
Number of Residues	20
Details	binding site for residue NAD G 301

Chain	Residue
C	TYR34
C	HIS38
C	PHE40
C	TYR148
C	GLY156
C	ASP181
G	PHE133
G	ASN137
G	ARG141
G	GLU166
G	PHE171
G	PHE172
G	THR173
G	LYS174
G	ASP177
G	ASP224
G	HIS261
G	LYS262
G	HOH407
G	HOH457

site_id	AC8
Number of Residues	17
Details	binding site for residue NAD H 301

Chain	Residue
E	TYR34
E	HIS38
E	PHE40
E	TYR148
E	GLY156
E	ASP181
H	PHE133
H	ASN137
H	ARG141
H	PHE171
H	PHE172
H	THR173
H	LYS174
H	HIS261
H	LYS262
H	HOH435
H	HOH459

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	80
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00193

Chain	Residue	Details
A	GLY47
A	HIS261
B	GLY47
B	ASP53
B	ARG141
B	THR161
B	GLU166
B	LYS174
B	ASP181
B	LYS190
B	THR212
A	ASP53
B	HIS261
C	GLY47
C	ASP53
C	ARG141
C	THR161
C	GLU166
C	LYS174
C	ASP181
C	LYS190
C	THR212
A	ARG141
C	HIS261
D	GLY47
D	ASP53
D	ARG141
D	THR161
D	GLU166
D	LYS174
D	ASP181
D	LYS190
D	THR212
A	THR161
D	HIS261
E	GLY47
E	ASP53
E	ARG141
E	THR161
E	GLU166
E	LYS174
E	ASP181
E	LYS190
E	THR212
A	GLU166
E	HIS261
F	GLY47
F	ASP53
F	ARG141
F	THR161
F	GLU166
F	LYS174
F	ASP181
F	LYS190
F	THR212
A	LYS174
F	HIS261
G	GLY47
G	ASP53
G	ARG141
G	THR161
G	GLU166
G	LYS174
G	ASP181
G	LYS190
G	THR212
A	ASP181
G	HIS261
H	GLY47
H	ASP53
H	ARG141
H	THR161
H	GLU166
H	LYS174
H	ASP181
H	LYS190
H	THR212
A	LYS190
H	HIS261
A	THR212

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)