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Crystal structure of rhesus macaque CD8 alpha-alpha homodimer

Analyse Crystal structure of rhesus macaque CD8 alpha-alpha homodimer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2Q3A
Type
protein
Length
231 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
CD8
Pockets
3 · best druggability 0.49

Structure

x-ray diffraction · 2 distinct chains · 3% helix, 46% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACD8protein1173% helix, 46% strand—
BCD8protein1143% helix, 46% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1890.490.8221empty
21280.390.7424empty
3940.350.7424empty

Interfaces

1 interface between chains.

  • A–B · 1170 Ų buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

  • 2Q3A · Crystal Structure of Rhesus Macaque CD8 Alpha-Alpha Homodimer · the same entry in another collection · chain A against A, TM-score 1.00

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