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Kshv lana (ORF73) C-terminal domain, decameric ring: orthorhombic crystal form

Analyse Kshv lana (ORF73) C-terminal domain, decameric ring: orthorhombic crystal form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2YPZ
Type
protein
Length
1,347 residues
Chains
10
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Kshv lana
UniProt
Q76SB0
Pockets
20 · best druggability 0.53

Structure

x-ray diffraction · 5 distinct chains · 32% helix, 22% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, C, D, G, I, JKshv lanaprotein13533% helix, 22% strandQ76SB0
BKshv lanaprotein13431% helix, 25% strandQ76SB0
EKshv lanaprotein13333% helix, 20% strandQ76SB0
FKshv lanaprotein13730% helix, 21% strandQ76SB0
HKshv lanaprotein13335% helix, 24% strandQ76SB0

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11580.530.8023empty
21520.530.8025empty
31470.500.7823empty
41360.490.7925empty
51110.470.7921empty

Interfaces

10 interfaces between chains.

  • C–D · 2276 Ų buried · 21 hydrogen bonds · protein-protein
  • A–B · 2185 Ų buried · 20 hydrogen bonds · protein-protein
  • I–J · 2146 Ų buried · 23 hydrogen bonds · protein-protein
  • E–F · 2136 Ų buried · 23 hydrogen bonds · protein-protein
  • G–H · 2004 Ų buried · 20 hydrogen bonds · protein-protein

Compared structures

  • 2YPZ · KSHV LANA (ORF73) C-terminal domain, decameric ring: orthorhombic crystal form · the same entry in another collection · chain C against C, TM-score 1.00

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