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Crystal structure of CMR6 from pyrococcus furiosus

Analyse Crystal structure of CMR6 from pyrococcus furiosus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4W8V
Type: protein
Length: 469 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: CRISPR system cmr subunit CMR6
UniProt: Q8U1T1
Pockets: 2 · best druggability 0.80

Structure

x-ray diffraction · 2 distinct chains · 38% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	CRISPR system cmr subunit CMR6	protein	237	38% helix, 19% strand	Q8U1T1
B	CRISPR system cmr subunit CMR6	protein	232	39% helix, 20% strand	Q8U1T1

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	832	0.80	0.82	80	empty
2	116	0.41	0.76	28	empty

Interfaces

1 interface between chains.

A–B · 2160 Å² buried · 29 hydrogen bonds · protein-protein

Compared structures

4W8V · Crystal structure of Cmr6 from Pyrococcus furiosus · the same entry in another collection · chain A against A, TM-score 1.00
Q8U1T1 · AlphaFold monomer V2.0 prediction for CRISPR system cmr subunit CMR6 (Q8U1T1) · a predicted model of the same protein · chain B against A, TM-score 0.80

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 Q8U1T1
Elsewhere: RCSB PDB 4W8V · PDBe 4W8V · UniProt Q8U1T1

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