Research workbench

Crystal structure of dimeric MERS-cov receptor binding domain

Analyse Crystal structure of dimeric MERS-cov receptor binding domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7C02
Type: protein
Length: 416 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Spike glycoprotein
UniProt: A0A0A0Q7F3
Ligands: NAG
Pockets: 3 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 16% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Spike glycoprotein	protein	208	16% helix, 36% strand	A0A0A0Q7F3

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A

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

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	348	0.66	0.80	33	empty
2	112	0.47	0.80	22	empty
3	69	0.31	0.74	17	empty

Interfaces

1 interface between chains.

A–B · 494 Å² buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide, 1 glycan (disulfide, N-glycosylation).

Compared structures

7C02 · Crystal structure of dimeric MERS-CoV receptor binding domain · 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 A0A0A0Q7F3
Elsewhere: RCSB PDB 7C02 · PDBe 7C02 · UniProt A0A0A0Q7F3

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.