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Solution structure of nelf E rrm

Analyse Solution structure of nelf E rrm in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2BZ2
Type: protein
Length: 79 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Negative elongation factor E
UniProt: P18615
Pockets: 1 · best druggability 0.38

Structure

solution nmr · 1 distinct chain · 24% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Negative elongation factor E	protein	79	24% helix, 25% strand	P18615

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	62	0.38	0.79	18	empty

Compared structures

2BZ2 · Solution structure of NELF E RRM · the same entry in another collection · chain A against A, TM-score 1.00
P18615 · AlphaFold monomer V2.0 prediction for negative elongation factor E (P18615) · a predicted model of the same protein · chain A against A, TM-score 0.83

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 P18615
Elsewhere: RCSB PDB 2BZ2 · PDBe 2BZ2 · UniProt P18615

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