MolNFT v1 · #154096 · protein

Crystal structure of CENAP1 core

6K02 · Nucleosome assembly protein: “Crystal structure of CENAP1 core”. X-ray diffraction, 1 ligand (ZN), 10 pockets (best druggability 0.47). MolNFT v1 #154096 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6K02
Type: protein
Length: 532 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nucleosome assembly protein
UniProt: Q19007
Ligands: ZN
Pockets: 10 · best druggability 0.47

Structure

x-ray diffraction · 2 distinct chains · 47% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Nucleosome assembly protein	protein	263	48% helix, 14% strand	Q19007
B	Nucleosome assembly protein	protein	269	47% helix, 16% strand	Q19007

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A, B

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

Pockets

10 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	160	0.47	0.77	19	empty
2	136	0.47	0.78	20	empty
3	240	0.47	0.73	28	empty
4	201	0.46	0.74	21	empty
5	197	0.46	0.74	21	empty

Interfaces

1 interface between chains.

A–B · 180 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

6K02 · Crystal structure of ceNAP1 core · 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 Q19007
Elsewhere: RCSB PDB 6K02 · PDBe 6K02 · UniProt Q19007

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