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Structure of the N-terminal domain of middle east respiratory syndrome coronavirus nucleocapsid protein

Analyse Structure of the N-terminal domain of middle east respiratory syndrome… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6KL2
Type: protein
Length: 442 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nucleoprotein
UniProt: A0A0D3MU65
Pockets: 3 · best druggability 0.67

Structure

x-ray diffraction · 3 distinct chains · 5% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Nucleoprotein	protein	116	5% helix, 23% strand	A0A0D3MU65
B	Nucleoprotein	protein	118	5% helix, 23% strand	A0A0D3MU65
C, D	Nucleoprotein	protein	104	6% helix, 22% strand	A0A0D3MU65

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	438	0.67	0.79	53	empty
2	93	0.42	0.78	25	empty
3	50	0.25	0.73	12	empty

Interfaces

3 interfaces between chains.

B–D · 549 Å² buried · 3 hydrogen bonds · protein-protein
A–C · 537 Å² buried · 3 hydrogen bonds · protein-protein
A–B · 270 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

6KL2 · Structure of the N-terminal domain of Middle East respiratory syndrome coronavirus… · 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 A0A0D3MU65
Elsewhere: RCSB PDB 6KL2 · PDBe 6KL2 · UniProt A0A0D3MU65

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