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Crystal structure of a CRISPR associated protein from thermus thermophilus HB8

Analyse Crystal structure of a CRISPR associated protein from thermus thermophilus HB8 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4EJ3
Type: protein
Length: 934 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: CRISPR associated protein
UniProt: Q53VY1
Pockets: 5 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	CRISPR associated protein	protein	467	46% helix, 17% strand	Q53VY1

Pockets

5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1081	0.70	0.74	117	empty
2	222	0.54	0.77	22	empty
3	84	0.52	0.85	22	empty
4	74	0.51	0.85	21	empty
5	57	0.26	0.73	17	empty

Interfaces

1 interface between chains.

A–B · 263 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

4EJ3 · Crystal structure of a CRISPR associated protein from Thermus thermophilus HB8 · the same entry in another collection · chain A against A, TM-score 1.00
Q53VY1 · AlphaFold monomer V2.0 prediction for CRISPR-associated protein CASA/CSE1 (Q53VY1) · a predicted model of the same protein · chain B 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 Q53VY1
Elsewhere: RCSB PDB 4EJ3 · PDBe 4EJ3 · UniProt Q53VY1

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