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Pandda analysis group deposition of models with modelled events (E.G. bound ligands) -- crystal structure of human FAM83B in complex with FF000014A

Analyse Pandda analysis group deposition of models with modelled events (E.G. bound… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5QHS
Type: protein
Length: 164 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein FAM83B
UniProt: Q5T0W9
Ligands: GQV
Pockets: 1 · best druggability 0.34

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein FAM83B	protein	164	35% helix, 30% strand	Q5T0W9

Ligands and binding sites

GQV · 1-methyl-3-oxidanyl-pyridin-2-one · ligand · chains A
EDO · 1,2-ethanediol · additive · 2 copies · chains A

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

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	60	0.34	0.77	16	EDO

Compared structures

5QHS · PanDDA analysis group deposition of models with modelled events (e.g. bound ligands)… · the same entry in another collection · chain A against A, TM-score 1.00
Q5T0W9 · AlphaFold monomer V2.0 prediction for protein FAM83B (Q5T0W9) · 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 Q5T0W9
Elsewhere: RCSB PDB 5QHS · PDBe 5QHS · UniProt Q5T0W9

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