MolNFT v2 · #220498 · protein

Cryo-EM structure of the RBD-ACE2 interface of the SARS-CoV-2 trimeric spike protein bound to ACE2 receptor after local refinement at downRBD conformation.

8T25 · Angiotensin-converting enzyme: “Cryo-EM structure of the RBD-ACE2 interface of the SARS-CoV-2 trimeric spike protein bound to ACE2 receptor…”. Electron microscopy at 3.62, 13 pockets (best druggability 0.77). MolNFT v2 #220498 on…

PDB: 8T25
Type: protein
Length: 787 residues
Chains: 2
Method: electron microscopy
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 3.62
Source: Neovison vison; Severe acute respiratory syndrome coronavirus 2
Molecule: Angiotensin-converting enzyme; Spike glycoprotein
UniProt: A0A7T0Q2W2, P0DTC2
Pockets: 13 · best druggability 0.77

Structure

electron microscopy · resolution 3.62 · 2 distinct chains · 48% helix, 6% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Angiotensin-converting enzyme	protein	595	60% helix, 2% strand	A0A7T0Q2W2
B	Spike glycoprotein	protein	192	11% helix, 19% strand	P0DTC2

Pockets

13 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	281	0.77	0.89	37	empty
2	768	0.76	0.80	76	empty
3	777	0.70	0.76	68	empty
4	61	0.69	0.96	22	empty
5	77	0.60	0.88	24	empty

Interfaces

1 interface between chains.

A–B · 925 Å² buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

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 A0A7T0Q2W2
Every structure of UniProt P0DTC2
Elsewhere: RCSB PDB 8T25 · PDBe 8T25 · UniProt A0A7T0Q2W2 · UniProt P0DTC2

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