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Coordinates of rrf and ef-G fitted into cryo-EM MAP of the 50S subunit bound with both ef-G (gdpnp) and rrf

Analyse Coordinates of rrf and ef-G fitted into cryo-EM MAP of the 50S subunit bound… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1ZN0
Type: protein
Length: 840 residues
Chains: 2
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ribosome recycling factor; Elongation factor G
UniProt: P0A805
Pockets: 3 · best druggability 0.43

Structure

electron microscopy · 2 distinct chains · 0% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ribosome recycling factor	protein	185	0% helix, 0% strand	P0A805
B	Elongation factor G	protein	655	0% helix, 0% strand	—

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	135	0.43	0.73	36	empty
2	69	0.33	0.73	20	empty
3	66	0.31	0.73	18	empty

Compared structures

1ZN0 · Coordinates of RRF and EF-G fitted into Cryo-EM map of the 50S subunit bound with both… · the same entry in another collection · chain A against A, TM-score 1.00
P0A805 · AlphaFold monomer V2.0 prediction for ribosome-recycling factor (P0A805) · a predicted model of the same protein · chain A against A, TM-score 0.62

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 P0A805
Elsewhere: RCSB PDB 1ZN0 · PDBe 1ZN0 · UniProt P0A805

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