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Trans-3/4-proline-hydroxylase H11 apo structure

Analyse Trans-3/4-proline-hydroxylase H11 apo structure in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7E05
Type
protein
Length
526 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Phytanoyl-CoA dioxygenase
UniProt
S5TUM1
Pockets
8 · best druggability 0.62

Structure

x-ray diffraction · 2 distinct chains · 25% helix, 23% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APhytanoyl-CoA dioxygenaseprotein26425% helix, 24% strandS5TUM1
BPhytanoyl-CoA dioxygenaseprotein26226% helix, 21% strandS5TUM1

Pockets

8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12460.620.8128empty
2950.580.8619empty
32040.520.7726empty
41970.520.7723empty
5520.480.8616empty

Interfaces

1 interface between chains.

  • A–B · 828 Ų buried · 17 hydrogen bonds · protein-protein

Compared structures

  • 7E05 · Trans-3/4-proline-hydroxylase H11 apo structure · the same entry in another collection · chain A against A, TM-score 1.00

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