Research workbench

X-ray structure of the YOS9 dimerization domain

Analyse X-ray structure of the YOS9 dimerization domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2YMA
Type: protein
Length: 267 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein os-9 homolog
UniProt: Q99220
Pockets: 4 · best druggability 0.44

Structure

x-ray diffraction · 2 distinct chains · 16% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein os-9 homolog	protein	135	14% helix, 36% strand	Q99220
B	Protein os-9 homolog	protein	132	19% helix, 36% strand	Q99220

Pockets

4 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	91	0.44	0.79	22	empty
2	85	0.39	0.77	21	empty
3	130	0.39	0.74	26	empty
4	122	0.38	0.74	27	empty

Interfaces

1 interface between chains.

A–B · 946 Å² buried · 22 hydrogen bonds · protein-protein

Compared structures

2YMA · X-ray structure of the Yos9 dimerization domain · the same entry in another collection · chain A against A, TM-score 1.00
Q99220 · AlphaFold monomer V2.0 prediction for protein os-9 homolog (Q99220) · a predicted model of the same protein · chain B against A, TM-score 0.97

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 Q99220
Elsewhere: RCSB PDB 2YMA · PDBe 2YMA · UniProt Q99220

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