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Crystal structure of MERS-cov NSP10/NSP16 complex bound to SAM

Analyse Crystal structure of MERS-cov NSP10/NSP16 complex bound to SAM in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5YN6
Type: protein
Length: 403 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: NSP16 protein; NSP10 protein
UniProt: K0BWD0, K4LC41
Ligands: SAM, ZN
Pockets: 3 · best druggability 0.45

Structure

x-ray diffraction · 2 distinct chains · 28% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	NSP16 protein	protein	283	30% helix, 22% strand	K0BWD0
B	NSP10 protein	protein	120	25% helix, 14% strand	K4LC41

Ligands and binding sites

SAM · S-adenosylmethionine · ligand · chains A
ZN · Zinc ion · metal · 2 copies · chains B

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

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	102	0.45	0.79	19	empty
2	120	0.40	0.75	30	SAM
3	52	0.28	0.75	13	empty

Interfaces

1 interface between chains.

A–B · 972 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

5YN6 · Crystal structure of MERS-CoV nsp10/nsp16 complex bound to SAM · 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 K0BWD0
Every structure of UniProt K4LC41
Elsewhere: RCSB PDB 5YN6 · PDBe 5YN6 · UniProt K0BWD0 · UniProt K4LC41

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