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Structure of the histidine tagged, open cytochrome P450 eryk from S. erythraea

Analyse Structure of the histidine tagged, open cytochrome P450 eryk from S. erythraea in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2WIO
Type: protein
Length: 393 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Erythromycin B/D C-12 hydroxylase
EC: 1.14.-.-
UniProt: P48635
Ligands: HEM
Pockets: 2 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 53% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Erythromycin B/D C-12 hydroxylase (EC 1.14.-.-)	protein	393	53% helix, 10% strand	P48635

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

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	955	0.79	0.80	89	HEM
2	59	0.38	0.80	13	empty

Compared structures

2WIO · Structure of the histidine tagged, open cytochrome P450 Eryk from S. erythraea · the same entry in another collection · chain A against A, TM-score 1.00
P48635 · AlphaFold monomer V2.0 prediction for erythromycin C-12 hydroxylase (P48635) · a predicted model of the same protein · chain A against A, TM-score 0.93

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P48635
Elsewhere: RCSB PDB 2WIO · PDBe 2WIO · UniProt P48635

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