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Schizosaccharomyces pombe CNP3 cupin domain

Analyse Schizosaccharomyces pombe CNP3 cupin domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6O2D
Type: protein
Length: 282 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Inner kinetochore subunit CNP3
UniProt: Q9USR9
Pockets: 3 · best druggability 0.45

Structure

x-ray diffraction · 2 distinct chains · 8% helix, 55% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Inner kinetochore subunit CNP3	protein	137	7% helix, 58% strand	Q9USR9
B	Inner kinetochore subunit CNP3	protein	145	9% helix, 52% strand	Q9USR9

Pockets

3 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	137	0.45	0.76	18	empty
2	62	0.34	0.76	12	empty
3	61	0.27	0.73	20	empty

Interfaces

1 interface between chains.

A–B · 2816 Å² buried · 33 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 modified (engineered).

Compared structures

6O2D · Schizosaccharomyces pombe Cnp3 Cupin Domain · the same entry in another collection · chain A against A, TM-score 1.00
Q9USR9 · AlphaFold monomer V2.0 prediction for inner kinetochore subunit CNP3 (Q9USR9) · a predicted model of the same protein · chain B against A, TM-score 0.99

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 Q9USR9
Elsewhere: RCSB PDB 6O2D · PDBe 6O2D · UniProt Q9USR9

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