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Model of full-length T. thermophilus translation initiation factor 2 refined against its cryo-EM density from a 30S initiation complex MAP

Analyse Model of full-length T. thermophilus translation initiation factor 2 refined… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3J4J
Type: protein
Length: 569 residues
Chains: 1
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Translation initiation factor if-2
UniProt: P48515
Pockets: 9 · best druggability 0.76

Structure

electron microscopy · 1 distinct chain · 27% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Translation initiation factor if-2	protein	569	27% helix, 22% strand	P48515

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	629	0.76	0.82	72	empty
2	70	0.56	0.87	22	empty
3	131	0.52	0.81	25	empty
4	59	0.43	0.82	21	empty
5	114	0.37	0.74	17	empty

Compared structures

3J4J · Model of full-length T. thermophilus Translation Initiation Factor 2 refined against its… · the same entry in another collection · chain A against A, TM-score 1.00
P48515 · AlphaFold monomer V2.0 prediction for translation initiation factor if-2 (P48515) · a predicted model of the same protein · chain A against A, TM-score 0.72

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 P48515
Elsewhere: RCSB PDB 3J4J · PDBe 3J4J · UniProt P48515

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