MolNFT v1 · #157529 · protein

Crystal structure of caenorhabditis elegans NAP1

6N2G · Nucleosome assembly protein: “Crystal structure of caenorhabditis elegans NAP1”. X-ray diffraction, 15 pockets (best druggability 0.82). MolNFT v1 #157529 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6N2G
Type: protein
Length: 1,112 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nucleosome assembly protein
UniProt: Q19007
Pockets: 15 · best druggability 0.82

Structure

x-ray diffraction · 3 distinct chains · 43% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Nucleosome assembly protein	protein	285	43% helix, 18% strand	Q19007
B, D	Nucleosome assembly protein	protein	273	44% helix, 19% strand	Q19007
C	Nucleosome assembly protein	protein	281	43% helix, 17% strand	Q19007

Pockets

15 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	1049	0.82	0.83	110	empty
2	950	0.72	0.76	73	empty
3	211	0.46	0.73	21	empty
4	221	0.46	0.73	28	empty
5	115	0.45	0.78	17	empty

Interfaces

5 interfaces between chains.

B–C · 4377 Å² buried · 54 hydrogen bonds · protein-protein
B–D · 588 Å² buried · 8 hydrogen bonds · protein-protein
A–C · 327 Å² buried · 4 hydrogen bonds · protein-protein
A–D · 250 Å² buried · 4 hydrogen bonds · protein-protein
C–D · 26 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

6N2G · Crystal structure of Caenorhabditis elegans NAP1 · 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 6N2G · PDBe 6N2G · UniProt Q19007

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