MolNFT v1 · #147891 · protein

Crystal structure of the human kinetochore protein cenp-N

6EQT · Centromere protein N: “Crystal structure of the human kinetochore protein cenp-N”. X-ray diffraction, 8 pockets (best druggability 0.64). MolNFT v1 #147891 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6EQT
Type: protein
Length: 412 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Centromere protein N
UniProt: Q96H22
Pockets: 8 · best druggability 0.64

Structure

x-ray diffraction · 2 distinct chains · 47% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Centromere protein N	protein	207	49% helix, 21% strand	Q96H22
B	Centromere protein N	protein	205	46% helix, 20% strand	Q96H22

Pockets

8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	290	0.64	0.81	25	empty
2	115	0.52	0.81	25	empty
3	87	0.43	0.79	13	empty
4	90	0.41	0.78	14	empty
5	56	0.34	0.78	13	empty

Interfaces

1 interface between chains.

A–B · 1104 Å² buried · 13 hydrogen bonds · protein-protein

Compared structures

6EQT · Crystal structure of the human kinetochore protein cenp-N · the same entry in another collection · chain A against A, TM-score 1.00
Q96H22 · AlphaFold monomer V2.0 prediction for centromere protein N (Q96H22) · a predicted model of the same protein · chain B against A, TM-score 0.96

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 Q96H22
Elsewhere: RCSB PDB 6EQT · PDBe 6EQT · UniProt Q96H22

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