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Structure of HIV-1 capsid protein by cryo-EM

Analyse Structure of HIV-1 capsid protein by cryo-EM in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3J34
Type
protein
Length
9,702 residues
Chains
42
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Capsid protein
UniProt
Q79791
Pockets
20 · best druggability 0.82

Structure

electron microscopy · 1 distinct chain · 54% helix, 2% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X, Y, Z, 5, a, b, c, 6, i, j, k, l, m, 7, d, e, f, g, hCapsid proteinprotein23154% helix, 2% strandQ79791

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110580.820.83127empty
211390.790.80128empty
36520.770.8280empty
49520.770.79102empty
511920.770.7990empty

Interfaces

83 interfaces between chains.

  • I–J · 1645 Ų buried · 10 hydrogen bonds · protein-protein
  • A–F · 1644 Ų buried · 12 hydrogen bonds · protein-protein
  • G–H · 1626 Ų buried · 15 hydrogen bonds · protein-protein
  • 5–a · 1618 Ų buried · 17 hydrogen bonds · protein-protein
  • 7–h · 1582 Ų buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 42 disulfide (disulfide).

Compared structures

  • 3J34 · Structure of HIV-1 Capsid Protein by Cryo-EM · the same entry in another collection · chain D against D, TM-score 1.00

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