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Crystal structure of isocitrate lyase from burkholderia pseudomallei

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

PDB: 3I4E
Type: protein
Length: 1,648 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Isocitrate lyase
EC: 4.1.3.1
UniProt: Q63SY3
Pockets: 20 · best druggability 0.90

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Isocitrate lyase (EC 4.1.3.1)	protein	412	51% helix, 12% strand	Q63SY3

Pockets

20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	986	0.90	0.93	157	empty
2	447	0.86	0.93	81	empty
3	615	0.84	0.89	85	empty
4	166	0.78	0.94	40	empty
5	92	0.72	0.95	26	empty

Interfaces

6 interfaces between chains.

B–C · 4365 Å² buried · 44 hydrogen bonds · protein-protein
A–D · 4307 Å² buried · 46 hydrogen bonds · protein-protein
B–D · 2254 Å² buried · 32 hydrogen bonds · protein-protein
A–C · 2222 Å² buried · 29 hydrogen bonds · protein-protein
A–B · 1033 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

3I4E · Crystal structure of Isocitrate Lyase from Burkholderia pseudomallei · 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 Q63SY3
Elsewhere: RCSB PDB 3I4E · PDBe 3I4E · UniProt Q63SY3

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