MolNFT v1 · #178431 · protein

Major cryo-EM structure of S protein trimer of SARS-COV2 with K-874, composite MAP

7FG3 · Spike glycoprotein: “Major cryo-EM structure of S protein trimer of SARS-COV2 with K-874, composite MAP”. Electron microscopy, 17 pockets (best druggability 0.74). MolNFT v1 #178431 on GenesisL1: 3D structure, binding sites and…

PDB: 7FG3
Type: protein
Length: 1,166 residues
Chains: 2
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Spike glycoprotein; K-874A vhh
UniProt: P0DTC2
Pockets: 17 · best druggability 0.74

Structure

electron microscopy · 2 distinct chains · 17% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Spike glycoprotein	protein	1050	18% helix, 17% strand	P0DTC2
D	K-874A vhh	protein	116	3% helix, 28% strand	—

Pockets

17 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	113	0.74	0.94	28	empty
2	237	0.71	0.86	33	empty
3	177	0.67	0.86	37	empty
4	174	0.67	0.86	26	empty
5	98	0.66	0.90	27	empty

Interfaces

1 interface between chains.

A–D · 721 Å² buried · 13 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 9 disulfide (disulfide).

Compared structures

7FG3 · Major cryo-EM structure of S protein trimer of SARS-CoV2 with K-874, composite map · 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 P0DTC2
Elsewhere: RCSB PDB 7FG3 · PDBe 7FG3 · UniProt P0DTC2

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