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Cryo-EM structure of isocitrate lyase-1 from candida albicans

Analyse Cryo-EM structure of isocitrate lyase-1 from candida albicans in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7EBF
Type: protein
Length: 1,640 residues
Chains: 4
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Isocitrate lyase
EC: 4.1.3.1
UniProt: Q59RB8
Pockets: 20 · best druggability 0.83

Structure

electron microscopy · 1 distinct chain · 49% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Isocitrate lyase (EC 4.1.3.1)	protein	410	49% helix, 13% strand	Q59RB8

Pockets

20 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	764	0.83	0.86	84	empty
2	799	0.82	0.85	90	empty
3	962	0.79	0.80	92	empty
4	742	0.78	0.82	84	empty
5	367	0.66	0.80	45	empty

Interfaces

4 interfaces between chains.

A–C · 1689 Å² buried · 35 hydrogen bonds · protein-protein
B–D · 1675 Å² buried · 34 hydrogen bonds · protein-protein
A–D · 797 Å² buried · 8 hydrogen bonds · protein-protein
B–C · 766 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

7EBF · Cryo-EM structure of Isocitrate lyase-1 from Candida albicans · 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 Q59RB8
Elsewhere: RCSB PDB 7EBF · PDBe 7EBF · UniProt Q59RB8

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