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Crystal structure of isocitrate lyase from mycobacterium tuberculosis

Analyse Crystal structure of isocitrate lyase from mycobacterium tuberculosis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1F61
Type: protein
Length: 836 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Isocitrate lyase
EC: 4.1.3.1
UniProt: P0A5H3
Ligands: MG
Pockets: 11 · best druggability 0.75

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Isocitrate lyase (EC 4.1.3.1)	protein	418	50% helix, 13% strand	P0A5H3

Ligands and binding sites

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

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	314	0.75	0.87	31	empty
2	293	0.61	0.79	36	MG
3	287	0.61	0.79	36	empty
4	107	0.52	0.82	26	empty
5	86	0.50	0.83	26	empty

Interfaces

1 interface between chains.

A–B · 4209 Å² buried · 60 hydrogen bonds · protein-protein

Compared structures

1F61 · Crystal structure of isocitrate lyase from mycobacterium tuberculosis · 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 P0A5H3
Elsewhere: RCSB PDB 1F61 · PDBe 1F61 · UniProt P0A5H3

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