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Crystal structure of a putative endoribonuclease (SO_1960) from shewanella oneidensis mr-1 at 1.85 a resolution

Analyse Crystal structure of a putative endoribonuclease (SO_1960) from shewanella… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2OTM
Type
protein
Length
456 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Hypothetical protein
UniProt
Q8EFL1
Ligands
NA, CA
Pockets
2 · best druggability 0.82

Structure

x-ray diffraction · 3 distinct chains · 37% helix, 27% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHypothetical proteinprotein15237% helix, 27% strandQ8EFL1
BHypothetical proteinprotein15337% helix, 27% strandQ8EFL1
CHypothetical proteinprotein15137% helix, 27% strandQ8EFL1

Ligands and binding sites

  • NA · Sodium ion · metal · 3 copies · chains A, B, C
  • CA · Calcium ion · metal · chains A, B, C
  • ACT · Acetate ion · additive · 6 copies · chains A, C, B
  • GOL · Glycerol · additive · chains B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11300.820.9926CA
2530.240.7224empty

Interfaces

3 interfaces between chains.

  • A–C · 1057 Ų buried · 16 hydrogen bonds · protein-protein
  • A–B · 1051 Ų buried · 18 hydrogen bonds · protein-protein
  • B–C · 1039 Ų buried · 17 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 modified (engineered).

Compared structures

  • 2OTM · Crystal structure of a putative endoribonuclease (so_1960) from shewanella oneidensis… · the same entry in another collection · chain A against A, TM-score 1.00

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