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Crystal structure of EFR3

Analyse Crystal structure of EFR3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4N5A
Type: protein
Length: 535 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein EFR3
UniProt: Q03653
Pockets: 3 · best druggability 0.30

Structure

x-ray diffraction · 1 distinct chain · 70% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein EFR3	protein	535	70% helix, 0% strand	Q03653

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	54	0.30	0.76	12	empty
2	57	0.28	0.74	11	empty
3	51	0.26	0.74	13	empty

Modifications

Observed in the structure: 13 modified (engineered).

Compared structures

4N5A · Crystal structure of Efr3 · the same entry in another collection · chain A against A, TM-score 1.00
Q03653 · AlphaFold monomer V2.0 prediction for protein EFR3 (Q03653) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q03653
Elsewhere: RCSB PDB 4N5A · PDBe 4N5A · UniProt Q03653

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