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Crystal structure of a putative endoribonuclease (TM0215) from thermotoga maritima MSB8 at 2.30 a resolution

Analyse Crystal structure of a putative endoribonuclease (TM0215) from thermotoga… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2B33
Type
protein
Length
253 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein synthesis inhibitor, putative
UniProt
Q9WY58
Ligands
CA
Pockets
3 · best druggability 0.59

Structure

x-ray diffraction · 2 distinct chains · 31% helix, 30% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein synthesis inhibitor, putativeprotein12731% helix, 30% strandQ9WY58
BProtein synthesis inhibitor, putativeprotein12631% helix, 30% strandQ9WY58

Ligands and binding sites

  • CA · Calcium ion · metal · chains B
  • EDO · 1,2-ethanediol · additive · 3 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11610.590.8330empty
2570.360.7915empty
3580.330.7716empty

Interfaces

1 interface between chains.

  • A–B · 513 Ų buried · 15 hydrogen bonds · protein-protein

Compared structures

  • 2B33 · Crystal structure of a putative endoribonuclease (TM0215) from thermotoga maritima MSB8… · the same entry in another collection · chain A against A, TM-score 1.00

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