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RNase 3/1 VERSION1

Analyse RNase 3/1 VERSION1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6YMT
Type
protein
Length
1,514 residues
Chains
12
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
RNase 3/1 version 1
Pockets
20 · best druggability 0.83

Structure

x-ray diffraction · 3 distinct chains · 22% helix, 32% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
G, F, H, LRNase 3/1 version 1protein12522% helix, 33% strand—
J, C, D, E, KRNase 3/1 version 1protein12621% helix, 32% strand—
A, I, BRNase 3/1 version 1protein12822% helix, 32% strand—

Ligands and binding sites

  • GOL · Glycerol · additive · chains A

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

Pockets

20 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13270.830.9336empty
26250.750.8188empty
37700.740.7959empty
46430.720.7960empty
59340.710.7673empty

Interfaces

22 interfaces between chains.

  • I–B · 697 Ų buried · 10 hydrogen bonds · protein-protein
  • D–E · 504 Ų buried · 5 hydrogen bonds · protein-protein
  • C–L · 497 Ų buried · 4 hydrogen bonds · protein-protein
  • J–F · 488 Ų buried · 5 hydrogen bonds · protein-protein
  • E–A · 468 Ų buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 48 disulfide (disulfide).

Compared structures

  • 6YMT · RNASE 3/1 version1 · the same entry in another collection · chain G against G, TM-score 1.00

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