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Crystal structure of C-terminal domain of ICP27 protein from HSV-1

Analyse Crystal structure of C-terminal domain of ICP27 protein from HSV-1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5BQK
Type
protein
Length
800 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
ICP27
UniProt
I3TCB5
Ligands
ZN
Pockets
10 · best druggability 0.73

Structure

x-ray diffraction · 2 distinct chains · 63% helix, 1% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, CICP27protein26763% helix, 1% strandI3TCB5
BICP27protein26663% helix, 1% strandI3TCB5

Ligands and binding sites

  • ZN · Zinc ion · metal · 3 copies · chains A, B, C

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

10 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17990.730.7896empty
25400.710.7943empty
31000.550.8418empty
41590.540.8034empty
5860.430.7915empty

Interfaces

2 interfaces between chains.

  • B–C · 5477 Ų buried · 64 hydrogen bonds · protein-protein
  • A–B · 589 Ų buried · 12 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 15 modified (engineered).

Compared structures

  • 5BQK · Crystal structure of C-terminal domain of ICP27 protein from HSV-1 · the same entry in another collection · chain A against A, TM-score 1.00

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