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Crystal structure and characterization of CMR5 protein from pyrococcus furiosus

Analyse Crystal structure and characterization of CMR5 protein 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: 4GKF
Type: protein
Length: 293 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: CRISPR system cmr subunit CMR5
UniProt: Q8U1T0
Pockets: 1 · best druggability 0.44

Structure

x-ray diffraction · 2 distinct chains · 73% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	CRISPR system cmr subunit CMR5	protein	146	73% helix, 0% strand	Q8U1T0
B	CRISPR system cmr subunit CMR5	protein	147	73% helix, 0% strand	Q8U1T0

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	113	0.44	0.77	20	empty

Interfaces

1 interface between chains.

A–B · 636 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

4GKF · Crystal structure and characterization of Cmr5 protein from Pyrococcus furiosus · the same entry in another collection · chain A against A, TM-score 1.00
Q8U1T0 · AlphaFold monomer V2.0 prediction for CRISPR system cmr subunit CMR5 (Q8U1T0) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 Q8U1T0
Elsewhere: RCSB PDB 4GKF · PDBe 4GKF · UniProt Q8U1T0

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