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Crystal structure of peptide releasing factor 1

Analyse Crystal structure of peptide releasing factor 1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1RQ0
Type: protein
Length: 947 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Peptide chain release factor 1
UniProt: Q9X183
Pockets: 14 · best druggability 0.46

Structure

x-ray diffraction · 2 distinct chains · 43% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Peptide chain release factor 1	protein	319	44% helix, 24% strand	Q9X183
B, C	Peptide chain release factor 1	protein	314	43% helix, 24% strand	Q9X183

Pockets

14 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	80	0.46	0.81	23	empty
2	110	0.45	0.78	21	empty
3	114	0.44	0.77	18	empty
4	124	0.44	0.77	25	empty
5	105	0.43	0.77	18	empty

Interfaces

2 interfaces between chains.

A–C · 992 Å² buried · 13 hydrogen bonds · protein-protein
A–B · 800 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

1RQ0 · Crystal structure of peptide releasing factor 1 · the same entry in another collection · chain A against A, TM-score 1.00
Q9X183 · AlphaFold monomer V2.0 prediction for peptide chain release factor 1 (Q9X183) · a predicted model of the same protein · chain B against A, TM-score 0.71

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 Q9X183
Elsewhere: RCSB PDB 1RQ0 · PDBe 1RQ0 · UniProt Q9X183

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