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Crystal structure of 8-mer peptide from rous sarcoma virus in complex with BF2*1201

Analyse Crystal structure of 8-mer peptide from rous sarcoma virus in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5YMW
Type
protein
Length
1,508 residues
Chains
12
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Class I histocompatibility antigen, F10 alpha chain; Beta-2-microglobulin…
UniProt
P15979, P21611
Pockets
15 · best druggability 0.80

Structure

x-ray diffraction · 3 distinct chains · 20% helix, 44% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, D, G, JClass I histocompatibility antigen, F10 alpha chainprotein27128% helix, 43% strandP15979
B, E, H, KBeta-2-microglobulinprotein980% helix, 50% strandP21611
C, F, I, LLeu-pro-ala-cys-val-leu-glu-valprotein80% helix, 0% strand—

Pockets

15 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19210.800.82101empty
26560.710.7951empty
34010.700.8247empty
44850.670.7851empty
52600.560.7732empty

Interfaces

16 interfaces between chains.

  • G–H · 1620 Ų buried · 21 hydrogen bonds · protein-protein
  • D–E · 1597 Ų buried · 20 hydrogen bonds · protein-protein
  • A–B · 1592 Ų buried · 26 hydrogen bonds · protein-protein
  • J–K · 1563 Ų buried · 27 hydrogen bonds · protein-protein
  • A–G · 940 Ų buried · 12 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 disulfide (disulfide).

Compared structures

  • 5YMW · Crystal structure of 8-mer peptide from Rous sarcoma virus in complex with BF2*1201 · the same entry in another collection · chain L against L, TM-score 1.00

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