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Crystal structure of a putative delta-5-3-ketosteroid isomerase (eca2236) from pectobacterium atrosepticum scri1043 at 1.55 A resolution

Analyse Crystal structure of a putative delta-5-3-ketosteroid isomerase (eca2236) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3F8X
Type
protein
Length
526 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
1.55
Source
Pectobacterium atrosepticum SCRI1043
Molecule
putative delta-5-3-ketosteroid isomerase
UniProt
Q6D504
Pockets
2 · best druggability 0.62

Structure

x-ray diffraction · resolution 1.55 · 3 distinct chains · 41% helix, 38% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
Aputative delta-5-3-ketosteroid isomeraseprotein13141% helix, 38% strandQ6D504
B, Dputative delta-5-3-ketosteroid isomeraseprotein13240% helix, 38% strandQ6D504
Cputative delta-5-3-ketosteroid isomeraseprotein13140% helix, 38% strandQ6D504

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14630.620.7652empty
2630.510.8522empty

Interfaces

5 interfaces between chains.

  • C–D · 1270 Ų buried · 12 hydrogen bonds · protein-protein
  • A–B · 1265 Ų buried · 11 hydrogen bonds · protein-protein
  • A–D · 217 Ų buried · 0 hydrogen bonds · protein-protein
  • A–C · 161 Ų buried · 0 hydrogen bonds · protein-protein
  • B–D · 159 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 16 modified (engineered).

Compared structures

  • 3F8X · Crystal structure of a putative delta-5-3-ketosteroid isomerase (ECA2236) from… · the same entry in another collection · chain A against A, TM-score 1.00

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