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Structure of P450PYR hydroxylase

Analyse Structure of P450PYR hydroxylase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3RWL
Type
protein
Length
404 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Cytochrome P450 alkane hydroxylase 1 CYP153A7
EC
1.14.15.3
UniProt
Q5F4D9
Ligands
HEM
Pockets
3 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 52% helix, 11% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACytochrome P450 alkane hydroxylase 1 CYP153A7 (EC 1.14.15.3)protein40452% helix, 11% strandQ5F4D9

Ligands and binding sites

  • HEM · Protoporphyrin IX containing Fe · ligand · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18030.780.8180HEM
2560.300.7513empty
3570.290.7516empty

Compared structures

  • 3RWL · Structure of P450pyr hydroxylase · the same entry in another collection · chain A against A, TM-score 1.00

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