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Crystal structure of the delta-pyrroline-5-carboxylate dehydrogenase from mycobacterium tuberculosis bound with NAD

Analyse Crystal structure of the delta-pyrroline-5-carboxylate dehydrogenase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4IHI
Type: protein
Length: 535 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Delta-1-pyrroline-5-carboxylate dehydrogenase
EC: 1.5.1.12
UniProt: O50443
Ligands: NAD
Pockets: 4 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Delta-1-pyrroline-5-carboxylate dehydrogenase (EC 1.5.1.12)	protein	535	42% helix, 20% strand	O50443

Ligands and binding sites

NAD · Nicotinamide-adenine-dinucleotide · ligand · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	961	0.81	0.82	109	NAD
2	143	0.39	0.73	22	empty
3	99	0.38	0.75	20	empty
4	80	0.33	0.75	20	empty

Compared structures

4IHI · Crystal structure of the Delta-pyrroline-5-carboxylate dehydrogenase from Mycobacterium… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt O50443
Elsewhere: RCSB PDB 4IHI · PDBe 4IHI · UniProt O50443

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