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NMR structure of the C-terminal region of human eukaryotic elongation factor 1B

Analyse NMR structure of the C-terminal region of human eukaryotic elongation factor 1B in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2N51
Type: protein
Length: 133 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Elongation factor 1-delta
UniProt: P29692
Pockets: 1 · best druggability 0.25

Structure

solution nmr · 1 distinct chain · 29% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Elongation factor 1-delta	protein	133	29% helix, 31% strand	P29692

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	57	0.25	0.73	13	empty

Compared structures

2N51 · NMR structure of the C-terminal region of human eukaryotic elongation factor 1B · the same entry in another collection · chain A against A, TM-score 1.00
P29692 · AlphaFold monomer V2.0 prediction for elongation factor 1-delta (P29692) · a predicted model of the same protein · chain A against A, TM-score 0.67

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 P29692
Elsewhere: RCSB PDB 2N51 · PDBe 2N51 · UniProt P29692

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