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Crystal structure of vaccinia virus polyadenylate POLYMERASE(VP55)

Analyse Crystal structure of vaccinia virus polyadenylate POLYMERASE(VP55) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3OWG
Type
protein
Length
914 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
POLY(A) polymerase catalytic subunit
EC
2.7.7.19
UniProt
P23371
Pockets
3 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BPOLY(A) polymerase catalytic subunit (EC 2.7.7.19)protein45746% helix, 15% strandP23371

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19190.820.84103empty
26140.730.8043empty
36230.730.8048empty

Interfaces

1 interface between chains.

  • A–B · 786 Ų buried · 7 hydrogen bonds · protein-protein

Compared structures

  • 3OWG · Crystal structure of vaccinia virus Polyadenylate polymerase(vp55) · the same entry in another collection · chain A against A, TM-score 1.00

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