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Crystal structure of the otu domain of otulin at 1.3 ångströms.

Analyse Crystal structure of the otu domain of otulin at 1.3 ångströms. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3ZNV
Type: protein
Length: 269 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein FAM105B
EC: 3.4.19.12
UniProt: Q96BN8
Ligands: CA, CL
Pockets: 2 · best druggability 0.42

Structure

x-ray diffraction · 1 distinct chain · 55% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein FAM105B (EC 3.4.19.12)	protein	269	55% helix, 12% strand	Q96BN8

Ligands and binding sites

CA · Calcium ion · metal · chains A
CL · Chloride ion · ion · chains A
GOL · Glycerol · additive · 4 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	65	0.42	0.81	13	empty
2	62	0.30	0.75	16	empty

Compared structures

3ZNV · Crystal structure of the OTU domain of OTULIN at 1.3 Angstroms. · the same entry in another collection · chain A against A, TM-score 1.00
Q96BN8 · AlphaFold monomer V2.0 prediction for ubiquitin thioesterase otulin (Q96BN8) · 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 Q96BN8
Elsewhere: RCSB PDB 3ZNV · PDBe 3ZNV · UniProt Q96BN8

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