GL1X · GenesisL1 explorer

MolNFT v2 · #188363 · protein

Structure of the mature RSV CA lattice: Group III, hexamer-hexamer interface, class 3'5

7NOE · Capsid protein p27, alternate cleaved 1: “Structure of the mature RSV CA lattice: Group III, hexamer-hexamer interface, class 3'5”. Electron microscopy at 7.5, 14 pockets (best druggability 0.58). MolNFT v2 #188363 on GenesisL1: 3D…

PDB
7NOE
Type
protein
Length
1,302 residues
Chains
10
Method
electron microscopy
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
7.5
Source
Rous sarcoma virus (strain Prague C)
Molecule
Capsid protein p27, alternate cleaved 1
UniProt
P03322
Pockets
14 · best druggability 0.58

Structure

electron microscopy · resolution 7.5 · 3 distinct chains · 66% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, D, G, ICapsid protein p27, alternate cleaved 1protein7863% helix, 0% strandP03322
B, ECapsid protein p27, alternate cleaved 1protein21766% helix, 0% strandP03322
C, F, H, JCapsid protein p27, alternate cleaved 1protein13968% helix, 0% strandP03322

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16110.580.73101empty
24630.540.7387empty
33830.510.7376empty
42540.460.7357empty
52730.460.7343empty

Interfaces

12 interfaces between chains.

  • B–C · 181 Ų buried · 0 hydrogen bonds · protein-protein
  • E–F · 165 Ų buried · 0 hydrogen bonds · protein-protein
  • D–G · 98 Ų buried · 1 hydrogen bond · protein-protein
  • A–B · 84 Ų buried · 0 hydrogen bonds · protein-protein
  • D–E · 83 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 7NOE · Structure of the mature rsv ca lattice: group III, hexamer-hexamer interface, class 3'5 · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

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