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Atomic resolution structures of escherichia COLI and bacillis anthracis malate synthase a: comparison with isoform G and implications for structure based drug design

Analyse Atomic resolution structures of escherichia COLI and bacillis anthracis malate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3CUX
Type: protein
Length: 501 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Malate synthase
EC: 2.3.3.9
UniProt: Q81TX1
Ligands: MG
Pockets: 5 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Malate synthase (EC 2.3.3.9)	protein	501	50% helix, 13% strand	Q81TX1

Ligands and binding sites

MG · Magnesium ion · metal · 2 copies · chains A

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

Pockets

5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	556	0.77	0.83	49	MG
2	158	0.52	0.79	24	empty
3	173	0.51	0.78	22	empty
4	115	0.42	0.77	17	empty
5	71	0.40	0.79	17	empty

Compared structures

3CUX · Atomic Resolution Structures of Escherichia coli and Bacillis anthracis Malate Synthase… · 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 Q81TX1
Elsewhere: RCSB PDB 3CUX · PDBe 3CUX · UniProt Q81TX1

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