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The CRISPR-associated CAS3 hd domain protein MJ0384 from methanocaldococcus jannaschii

Analyse The CRISPR-associated CAS3 hd domain protein MJ0384 from methanocaldococcus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3S4L
Type: protein
Length: 197 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: CAS3 metal dependent phosphohydrolase
UniProt: Q57829
Ligands: CA
Pockets: 2 · best druggability 0.57

Structure

x-ray diffraction · 1 distinct chain · 66% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	CAS3 metal dependent phosphohydrolase	protein	197	66% helix, 4% strand	Q57829

Ligands and binding sites

CA · Calcium ion · metal · 2 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

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	206	0.57	0.80	25	empty
2	53	0.30	0.75	14	empty

Compared structures

3S4L · The CRISPR-associated Cas3 HD domain protein MJ0384 from Methanocaldococcus jannaschii · the same entry in another collection · chain A against A, TM-score 1.00
Q57829 · AlphaFold monomer V2.0 prediction for CRISPR-associated endonuclease CAS3-hd (Q57829) · a predicted model of the same protein · chain A against A, TM-score 0.95

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 Q57829
Elsewhere: RCSB PDB 3S4L · PDBe 3S4L · UniProt Q57829

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