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Asymmetric unit for phage qbeta small prolate particle

Analyse Asymmetric unit for phage qbeta small prolate particle in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7LGH
Type
protein
Length
2,904 residues
Chains
22
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Capsid protein
UniProt
P03615
Pockets
20 · best druggability 0.73

Structure

electron microscopy · 1 distinct chain · 22% helix, 40% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, L, D, M, E, N, F, O, G, P, H, Q, R, I, S, J, T, U, K, VCapsid proteinprotein13222% helix, 40% strandP03615

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13210.730.8551empty
27950.720.7778empty
32890.680.8348empty
44830.680.7963empty
53860.660.8038empty

Interfaces

65 interfaces between chains.

  • A–B · 3543 Ų buried · 42 hydrogen bonds · protein-protein
  • G–P · 3538 Ų buried · 46 hydrogen bonds · protein-protein
  • H–Q · 3524 Ų buried · 36 hydrogen bonds · protein-protein
  • E–N · 3494 Ų buried · 46 hydrogen bonds · protein-protein
  • F–O · 3494 Ų buried · 44 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 15 disulfide (disulfide).

Compared structures

  • 7LGH · Asymmetric unit for phage Qbeta small prolate particle · the same entry in another collection · chain A against A, TM-score 1.00

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