Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4NS3

Crystal structure of the Delta-pyrroline-5-carboxylate dehydrogenase from Mycobacterium tuberculosis bound with NAD and cobalamin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0003842	molecular_function	1-pyrroline-5-carboxylate dehydrogenase activity
A	0006560	biological_process	proline metabolic process
A	0009898	cellular_component	cytoplasmic side of plasma membrane
A	0010133	biological_process	proline catabolic process to glutamate
A	0016491	molecular_function	oxidoreductase activity
A	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
A	0046872	molecular_function	metal ion binding
B	0000166	molecular_function	nucleotide binding
B	0003842	molecular_function	1-pyrroline-5-carboxylate dehydrogenase activity
B	0006560	biological_process	proline metabolic process
B	0009898	cellular_component	cytoplasmic side of plasma membrane
B	0010133	biological_process	proline catabolic process to glutamate
B	0016491	molecular_function	oxidoreductase activity
B	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
B	0046872	molecular_function	metal ion binding
C	0000166	molecular_function	nucleotide binding
C	0003842	molecular_function	1-pyrroline-5-carboxylate dehydrogenase activity
C	0006560	biological_process	proline metabolic process
C	0009898	cellular_component	cytoplasmic side of plasma membrane
C	0010133	biological_process	proline catabolic process to glutamate
C	0016491	molecular_function	oxidoreductase activity
C	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
C	0046872	molecular_function	metal ion binding
D	0000166	molecular_function	nucleotide binding
D	0003842	molecular_function	1-pyrroline-5-carboxylate dehydrogenase activity
D	0006560	biological_process	proline metabolic process
D	0009898	cellular_component	cytoplasmic side of plasma membrane
D	0010133	biological_process	proline catabolic process to glutamate
D	0016491	molecular_function	oxidoreductase activity
D	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
D	0046872	molecular_function	metal ion binding
E	0000166	molecular_function	nucleotide binding
E	0003842	molecular_function	1-pyrroline-5-carboxylate dehydrogenase activity
E	0006560	biological_process	proline metabolic process
E	0009898	cellular_component	cytoplasmic side of plasma membrane
E	0010133	biological_process	proline catabolic process to glutamate
E	0016491	molecular_function	oxidoreductase activity
E	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
E	0046872	molecular_function	metal ion binding
F	0000166	molecular_function	nucleotide binding
F	0003842	molecular_function	1-pyrroline-5-carboxylate dehydrogenase activity
F	0006560	biological_process	proline metabolic process
F	0009898	cellular_component	cytoplasmic side of plasma membrane
F	0010133	biological_process	proline catabolic process to glutamate
F	0016491	molecular_function	oxidoreductase activity
F	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
F	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	26
Details	BINDING SITE FOR RESIDUE B12 A 601

Chain	Residue
A	ILE186
A	HOH750
A	HOH770
A	HOH771
A	HOH798
A	HOH864
A	HOH876
A	HOH935
A	HOH970
A	HOH1007
A	HOH1015
A	PHE246
A	HOH1022
A	HOH1080
A	HOH1174
C	LYS386
C	GLU398
C	TYR399
C	HOH1063
A	ASP250
A	ALA268
A	THR269
A	HIS272
A	HOH701
A	HOH720
A	HOH746

site_id	AC2
Number of Residues	20
Details	BINDING SITE FOR RESIDUE B12 B 601

Chain	Residue
B	PHE246
B	ASP250
B	THR269
B	HIS272
B	ARG373
B	HOH714
B	HOH750
B	HOH767
B	HOH771
B	HOH775
B	HOH794
B	HOH842
B	HOH843
B	HOH993
B	HOH1049
B	HOH1080
B	HOH1117
B	HOH1138
C	ASP37
C	PRO39

site_id	AC3
Number of Residues	15
Details	BINDING SITE FOR RESIDUE B12 C 601

Chain	Residue
C	PHE246
C	ASP250
C	THR269
C	HIS272
C	ARG373
C	HOH766
C	HOH776
C	HOH815
C	HOH822
C	HOH985
C	HOH1000
C	HOH1074
C	HOH1162
D	ASN280
D	ARG283

site_id	AC4
Number of Residues	27
Details	BINDING SITE FOR RESIDUE B12 D 601

Chain	Residue
C	ALA79
C	ASP250
C	VAL251
C	ALA254
C	ASP255
C	PRO256
C	ARG283
D	ILE186
D	PHE246
D	ASP250
D	ALA268
D	THR269
D	HIS272
D	ARG373
D	HOH703
D	HOH737
D	HOH778
D	HOH795
D	HOH801
D	HOH891
D	HOH931
D	HOH961
D	HOH994
D	HOH1054
D	HOH1058
D	HOH1061
D	HOH1139

site_id	AC5
Number of Residues	16
Details	BINDING SITE FOR RESIDUE NAD E 601

Chain	Residue
E	SER266
E	THR269
E	HIS272
E	HOH998
E	HOH1016
E	TYR184
E	ILE186
E	THR187
E	PRO188
E	PHE189
E	ASN190
E	LYS212
E	SER214
E	GLY245
E	SER249
E	PHE263

site_id	AC6
Number of Residues	17
Details	BINDING SITE FOR RESIDUE NAD F 601

Chain	Residue
F	TYR184
F	ILE186
F	THR187
F	PHE189
F	ASN190
F	LYS212
F	SER214
F	GLY245
F	SER249
F	PHE263
F	GLY265
F	SER266
F	THR269
F	HIS272
F	CME327
F	HOH891
F	HOH1032

Functional Information from PROSITE/UniProt

site_id	PS00070
Number of Residues	12
Details	ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FdYQGQKCSAVS

Chain	Residue	Details
A	PHE320-SER331

site_id	PS00687
Number of Residues	8
Details	ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. GETGGKDF

Chain	Residue	Details
A	GLY292-PHE299

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