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Hydroxylase domain of SCS7P

Analyse Hydroxylase domain of SCS7P in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4ZR1
Type
protein
Length
549 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ceramide very long chain fatty acid hydroxylase SCS7
EC
1.-.-.-
UniProt
Q03529
Ligands
TRD, ZN
Pockets
9 · best druggability 0.80

Structure

x-ray diffraction · 2 distinct chains · 58% helix, 1% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACeramide very long chain fatty acid hydroxylase SCS7 (EC 1.-.-.-)protein27458% helix, 1% strandQ03529
BCeramide very long chain fatty acid hydroxylase SCS7 (EC 1.-.-.-)protein27557% helix, 1% strandQ03529

Ligands and binding sites

  • TRD · Tridecane · ligand · 8 copies · chains A, B
  • ZN · Zinc ion · metal · 4 copies · chains A, B
  • BOG · octyl beta-D-glucopyranoside · additive · 8 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18710.800.8292BOG, TRD
28980.790.8156BOG, TRD
31650.670.8626TRD
41180.530.8226empty
51170.490.8024empty

Interfaces

1 interface between chains.

  • A–B · 476 Ų buried · 1 hydrogen bond · protein-protein

Compared structures

  • 4ZR1 · Hydroxylase domain of scs7p · the same entry in another collection · chain A against A, TM-score 1.00
  • Q03529 · AlphaFold monomer V2.0 prediction for ceramide very long chain fatty acid hydroxylase… · a predicted model of the same protein · chain A against A, TM-score 0.98

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