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Crystal structure of synthetic HIV-1 capsid C-terminal domain (cca)

Analyse Crystal structure of synthetic HIV-1 capsid C-terminal domain (cca) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3LRY
Type
protein
Length
142 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
HIV-1 capsid protein
UniProt
Q71B91
Pockets
2 · best druggability 0.46

Structure

x-ray diffraction · 1 distinct chain · 66% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BHIV-1 capsid proteinprotein7166% helix, 0% strandQ71B91

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11040.460.7916empty
2530.320.7717empty

Interfaces

1 interface between chains.

  • A–B · 473 Ų buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

  • 3LRY · Crystal structure of synthetic HIV-1 capsid C-terminal domain (CCA) · the same entry in another collection · chain A against A, TM-score 1.00

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