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Crystal structure of mycobacterium tuberculosis malate synthase in complex with 4-(2-mehtylphenyl)-2,4-dioxobutanoic acid inhibitor

Analyse Crystal structure of mycobacterium tuberculosis malate synthase in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3SAD
Type: protein
Length: 709 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Malate synthase G
EC: 2.3.3.9
UniProt: P0A5J4
Ligands: 040, MG
Pockets: 10 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Malate synthase G (EC 2.3.3.9)	protein	709	47% helix, 18% strand	P0A5J4

Ligands and binding sites

040 · 4-(2-methylphenyl)-2,4-dioxobutanoic acid · ligand · chains A
MG · Magnesium ion · metal · 3 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	97	0.76	0.97	27	MG, 040
2	340	0.60	0.77	35	empty
3	136	0.52	0.80	33	empty
4	54	0.51	0.87	18	empty
5	166	0.50	0.77	32	empty

Compared structures

3SAD · Crystal structure of Mycobacterium tuberculosis malate synthase in complex with… · 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 P0A5J4
Elsewhere: RCSB PDB 3SAD · PDBe 3SAD · UniProt P0A5J4

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