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Crystal structure of ELMO2(ENGULFMENT and cell motility protein 2)

Analyse Crystal structure of ELMO2(ENGULFMENT and cell motility protein 2) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6IE1
Type: protein
Length: 508 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Engulfment and cell motility protein 2
UniProt: Q96JJ3
Pockets: 6 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 61% helix, 6% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Engulfment and cell motility protein 2	protein	508	61% helix, 6% strand	Q96JJ3

Ligands and binding sites

GOL · Glycerol · additive · 2 copies · chains A

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

Pockets

6 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	296	0.75	0.87	32	GOL
2	95	0.58	0.86	18	empty
3	51	0.41	0.82	11	empty
4	65	0.38	0.79	20	empty
5	60	0.34	0.77	13	empty

Compared structures

6IE1 · Crystal Structure of ELMO2(Engulfment and cell motility protein 2) · the same entry in another collection · chain A against A, TM-score 1.00
Q96JJ3 · AlphaFold monomer V2.0 prediction for engulfment and cell motility protein 2 (Q96JJ3) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 Q96JJ3
Elsewhere: RCSB PDB 6IE1 · PDBe 6IE1 · UniProt Q96JJ3

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