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Crystal structure analysis of chus, an E. COLI heme oxygenase

Analyse Crystal structure analysis of chus, an E. COLI heme oxygenase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1U9T
Type
protein
Length
327 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Putative HEME/HEMOGLOBIN transport protein
UniProt
Q8X5N8
Pockets
3 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 25% helix, 33% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APutative HEME/HEMOGLOBIN transport proteinprotein32725% helix, 33% strandQ8X5N8

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17040.720.7866empty
21850.480.7626empty
3690.340.7624empty

Compared structures

  • 1U9T · Crystal Structure Analysis of ChuS, an E. coli Heme Oxygenase · the same entry in another collection · chain A against A, TM-score 1.00

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