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Cryo-EM structure of OTOP3 from xenopus tropicalis

Analyse Cryo-EM structure of OTOP3 from xenopus tropicalis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6O84
Type: protein
Length: 830 residues
Chains: 2
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: LOC100127796 PROTEIN,LOC100127796 PROTEIN,OTOP3, LOC100127796 PROTEIN,LOC100127796 protein
UniProt: A9JTM7
Pockets: 12 · best druggability 0.79

Structure

electron microscopy · 1 distinct chain · 75% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	LOC100127796 PROTEIN,LOC100127796 PROTEIN,OTOP3, LOC100127796 PROTEIN,LOC100127796 protein	protein	415	75% helix, 1% strand	A9JTM7

Pockets

12 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	577	0.79	0.85	57	empty
2	542	0.78	0.84	49	empty
3	846	0.77	0.81	73	empty
4	810	0.76	0.80	71	empty
5	921	0.75	0.78	72	empty

Interfaces

1 interface between chains.

A–B · 1666 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

6O84 · Cryo-EM structure of OTOP3 from xenopus tropicalis · 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 A9JTM7
Elsewhere: RCSB PDB 6O84 · PDBe 6O84 · UniProt A9JTM7

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