MolNFT v1 · #83868 · protein

Crystal structure of thermobifida fusca CSE1

3WVO · CRISPR-associated protein, CSE1 family: “Crystal structure of thermobifida fusca CSE1”. X-ray diffraction, 20 pockets (best druggability 0.79). MolNFT v1 #83868 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 3WVO
Type: protein
Length: 1,625 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: CRISPR-associated protein, CSE1 family
UniProt: Q47PI4
Pockets: 20 · best druggability 0.79

Structure

x-ray diffraction · 3 distinct chains · 43% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	CRISPR-associated protein, CSE1 family	protein	543	44% helix, 13% strand	Q47PI4
B	CRISPR-associated protein, CSE1 family	protein	542	43% helix, 13% strand	Q47PI4
C	CRISPR-associated protein, CSE1 family	protein	540	43% helix, 13% strand	Q47PI4

Pockets

20 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	608	0.79	0.84	72	empty
2	239	0.61	0.81	35	empty
3	217	0.61	0.81	35	empty
4	293	0.61	0.79	37	empty
5	88	0.59	0.88	28	empty

Interfaces

2 interfaces between chains.

A–B · 1543 Å² buried · 14 hydrogen bonds · protein-protein
A–C · 514 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

3WVO · Crystal structure of Thermobifida fusca Cse1 · the same entry in another collection · chain A against A, TM-score 1.00

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 Q47PI4
Elsewhere: RCSB PDB 3WVO · PDBe 3WVO · UniProt Q47PI4

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