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Crystal structure of mycobacterium tuberculosis malate synthase in complex with 3-(PHENYLTHIO)ACRYLIC acid

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: 5CBJ
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: P9WK17
Ligands: 4ZD, MG
Pockets: 4 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Malate synthase G (EC 2.3.3.9)	protein	709	47% helix, 17% strand	P9WK17

Ligands and binding sites

4ZD · (2E)-3-(phenylsulfanyl)prop-2-enoic acid · ligand · chains A
MG · Magnesium ion · metal · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	635	0.75	0.81	65	MG, 4ZD
2	125	0.50	0.80	28	empty
3	123	0.46	0.78	31	empty
4	55	0.41	0.82	20	empty

Compared structures

P9WK17 · AlphaFold monomer V2.0 prediction for malate synthase G (P9WK17) · a predicted model of the same protein · 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 P9WK17
Elsewhere: RCSB PDB 5CBJ · PDBe 5CBJ · UniProt P9WK17

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