Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6OFC

Crystal structure of M. tuberculosis glutamine-dependent NAD+ synthetase complexed with Sulfonamide derivative 1, pyrophosphate, and glutamine

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	0005886	cellular_component	plasma membrane
A	0008795	molecular_function	NAD+ synthase activity
A	0009274	cellular_component	peptidoglycan-based cell wall
A	0009435	biological_process	NAD+ biosynthetic process
A	0016874	molecular_function	ligase activity
A	0042802	molecular_function	identical protein 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	0005886	cellular_component	plasma membrane
B	0008795	molecular_function	NAD+ synthase activity
B	0009274	cellular_component	peptidoglycan-based cell wall
B	0009435	biological_process	NAD+ biosynthetic process
B	0016874	molecular_function	ligase activity
B	0042802	molecular_function	identical protein 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	0005886	cellular_component	plasma membrane
C	0008795	molecular_function	NAD+ synthase activity
C	0009274	cellular_component	peptidoglycan-based cell wall
C	0009435	biological_process	NAD+ biosynthetic process
C	0016874	molecular_function	ligase activity
C	0042802	molecular_function	identical protein 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	0005886	cellular_component	plasma membrane
D	0008795	molecular_function	NAD+ synthase activity
D	0009274	cellular_component	peptidoglycan-based cell wall
D	0009435	biological_process	NAD+ biosynthetic process
D	0016874	molecular_function	ligase activity
D	0042802	molecular_function	identical protein binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	binding site for residue SFH A 701

Chain	Residue
A	GLY366
A	TRP490
A	SER491
A	THR492
A	ASP497
A	HOH803
A	VAL367
A	SER368
A	SER373
A	PHE397
A	ALA398
A	LEU399
A	ARG462
A	THR480

site_id	AC2
Number of Residues	11
Details	binding site for residue SFH A 702

Chain	Residue
A	ASN456
A	THR492
A	TYR493
A	PHE634
A	LYS635
A	SER661
D	ARG354
D	LEU358
D	ASN471
D	GLY475
D	HIS501

site_id	AC3
Number of Residues	17
Details	binding site for residue SFH A 703

Chain	Residue
A	ARG354
A	LEU358
A	ASN471
A	GLY475
A	ILE476
A	HIS501
D	ASN456
D	GLY489
D	SER491
D	THR492
D	TYR493
D	ARG627
D	PHE631
D	PHE634
D	LYS635
D	SER661
D	SFH701

site_id	AC4
Number of Residues	1
Details	binding site for residue CL A 705

Chain	Residue
A	MET663

site_id	AC5
Number of Residues	16
Details	binding site for residue SFH B 701

Chain	Residue
B	GLY366
B	VAL367
B	SER368
B	SER373
B	PHE397
B	ALA398
B	LEU399
B	ARG462
B	THR480
B	TRP490
B	SER491
B	THR492
B	ASP497
B	GLU552
B	POP705
B	HOH806

site_id	AC6
Number of Residues	13
Details	binding site for residue SFH B 702

Chain	Residue
B	ASN456
B	THR492
B	TYR493
B	PHE631
B	PHE634
B	LYS635
B	SER661
B	HOH807
C	ARG354
C	LEU358
C	ASN471
C	GLY475
C	HIS501

site_id	AC7
Number of Residues	10
Details	binding site for residue SFH B 703

Chain	Residue
B	ARG354
B	LEU358
B	ASN471
B	GLY475
B	ILE476
B	HIS501
C	ASN456
C	TYR493
C	PHE634
C	LYS635

site_id	AC8
Number of Residues	1
Details	binding site for residue CL B 704

Chain	Residue
B	MET499

site_id	AC9
Number of Residues	10
Details	binding site for residue POP B 705

Chain	Residue
B	SER368
B	GLY370
B	LEU371
B	ASP372
B	SER373
B	GLU541
B	GLU552
B	GLU553
B	LEU554
B	SFH701

site_id	AD1
Number of Residues	3
Details	binding site for residue GLN B 706

Chain	Residue
B	ARG218
D	LEU215
D	ARG218

site_id	AD2
Number of Residues	6
Details	binding site for residue GOL B 707

Chain	Residue
A	ASP656
B	ASP62
B	ARG134
A	ARG128
A	ARG285
A	LEU575

site_id	AD3
Number of Residues	13
Details	binding site for residue SFH C 701

Chain	Residue
C	GLY366
C	VAL367
C	SER368
C	SER373
C	PHE397
C	ALA398
C	LEU399
C	ARG462
C	THR480
C	TRP490
C	SER491
C	THR492
C	ASP497

site_id	AD4
Number of Residues	12
Details	binding site for residue GLN C 702

Chain	Residue
C	GLU52
C	TYR58
C	LYS121
C	PRO125
C	TYR127
C	PHE130
C	ALA176
C	GLU177
C	PHE180
C	SER203
C	ARG209
C	HOH801

site_id	AD5
Number of Residues	10
Details	binding site for residue SFH D 701

Chain	Residue
A	SFH703
D	GLY366
D	VAL367
D	SER368
D	PHE397
D	LEU399
D	ARG462
D	THR480
D	TRP490
D	THR492

site_id	AD6
Number of Residues	3
Details	binding site for residue CL D 702

Chain	Residue
D	THR463
D	ASP497
D	MET499

site_id	AD7
Number of Residues	5
Details	binding site for residue GLN D 703

Chain	Residue
D	TYR127
D	GLU177
D	PHE180
D	SER203
D	ARG209

site_id	AD8
Number of Residues	6
Details	binding site for residue GOL D 704

Chain	Residue
A	LEU65
A	ARG134
B	ARG128
D	ARG285
D	LEU575
D	ASP656

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1056
Details	Domain: {"description":"CN hydrolase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00054","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	76
Details	Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Active site: {"description":"Proton acceptor; for glutaminase activity","evidences":[{"source":"HAMAP-Rule","id":"MF_02090","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15748981","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"19270703","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Active site: {"description":"For glutaminase activity","evidences":[{"source":"HAMAP-Rule","id":"MF_02090","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15748981","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"19270703","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	4
Details	Active site: {"description":"Nucleophile; for glutaminase activity","evidences":[{"source":"HAMAP-Rule","id":"MF_02090","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15748981","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"19270703","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02090","evidenceCode":"ECO:0000255"},{"source":"PDB","id":"3SYT","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	28
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02090","evidenceCode":"ECO:0000255"},{"source":"PDB","id":"3SEQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SEZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SYT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SZG","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	4
Details	Binding site: {"description":"in other chain","evidences":[{"source":"HAMAP-Rule","id":"MF_02090","evidenceCode":"ECO:0000255"},{"source":"PDB","id":"3DLA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SEQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SEZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SZG","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02090","evidenceCode":"ECO:0000255"},{"source":"PDB","id":"3SEQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SYT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SZG","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	4
Details	Binding site: {"description":"in other chain","evidences":[{"source":"HAMAP-Rule","id":"MF_02090","evidenceCode":"ECO:0000255"},{"source":"PDB","id":"3SEQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SEZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SYT","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	16
Details	Binding site: {"description":"in other chain","evidences":[{"source":"HAMAP-Rule","id":"MF_02090","evidenceCode":"ECO:0000255"},{"source":"PDB","id":"3DLA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SEQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SEZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SYT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SZG","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PDB","id":"3DLA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SEQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SEZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SYT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SZG","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	4
Details	Binding site: {"description":"in other chain","evidences":[{"source":"PDB","id":"3DLA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SZG","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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