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2.0A crystal structure of isocitrate lyase from brucella melitensis (P43212)

Analyse 2.0A crystal structure of isocitrate lyase from brucella melitensis (P43212) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3EOL
Type: protein
Length: 724 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Isocitrate lyase
EC: 4.1.3.1
UniProt: Q8YIN4
Pockets: 3 · best druggability 0.73

Structure

x-ray diffraction · 2 distinct chains · 50% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Isocitrate lyase (EC 4.1.3.1)	protein	362	50% helix, 13% strand	Q8YIN4
B	Isocitrate lyase (EC 4.1.3.1)	protein	362	50% helix, 13% strand	Q8YIN4

Ligands and binding sites

PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains B
GOL · Glycerol · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	661	0.73	0.80	58	empty
2	66	0.34	0.77	16	empty
3	64	0.31	0.75	16	empty

Interfaces

1 interface between chains.

A–B · 402 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

3EOL · 2.0A crystal structure of isocitrate lyase from Brucella melitensis (P43212) · 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 Q8YIN4
Elsewhere: RCSB PDB 3EOL · PDBe 3EOL · UniProt Q8YIN4

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