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1.4A crystal structure of isocitrate lyase from yersinia pestis CO92

Analyse 1.4A crystal structure of isocitrate lyase from yersinia pestis CO92 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3LG3
Type: protein
Length: 833 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Isocitrate lyase
EC: 4.1.3.1
UniProt: Q7CLE1
Pockets: 15 · best druggability 0.81

Structure

x-ray diffraction · 2 distinct chains · 51% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Isocitrate lyase (EC 4.1.3.1)	protein	419	51% helix, 13% strand	Q7CLE1
B	Isocitrate lyase (EC 4.1.3.1)	protein	414	51% helix, 13% strand	Q7CLE1

Pockets

15 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	1173	0.81	0.82	120	empty
2	168	0.51	0.78	31	empty
3	159	0.48	0.78	24	empty
4	131	0.41	0.75	29	empty
5	87	0.41	0.78	16	empty

Interfaces

1 interface between chains.

A–B · 752 Å² buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 18 modified (engineered).

Compared structures

3LG3 · 1.4A Crystal Structure of Isocitrate Lyase from Yersinia pestis CO92 · 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 Q7CLE1
Elsewhere: RCSB PDB 3LG3 · PDBe 3LG3 · UniProt Q7CLE1

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