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Crystal structure of ef-pyl

Analyse Crystal structure of ef-pyl in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3WND
Type: protein
Length: 361 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein translation elongation factor 1A
UniProt: Q8PXB3
Pockets: 4 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 20% helix, 42% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein translation elongation factor 1A	protein	361	20% helix, 42% strand	Q8PXB3

Ligands and binding sites

CIT · Citric acid · additive · 2 copies · chains A

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

Pockets

4 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	353	0.65	0.79	30	empty
2	145	0.49	0.78	20	empty
3	55	0.37	0.80	21	empty
4	53	0.27	0.73	12	empty

Compared structures

3WND · Crystal structure of EF-Pyl · 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 Q8PXB3
Elsewhere: RCSB PDB 3WND · PDBe 3WND · UniProt Q8PXB3

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