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Solution conformation of cytochrome P450 mycg with mycinamicin IV bound

Analyse Solution conformation of cytochrome P450 mycg with mycinamicin IV bound in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5UHU
Type: protein
Length: 393 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Mycinamicin IV HYDROXYLASE/EPOXIDASE
EC: 1.14.-.-
UniProt: Q59523
Ligands: HEM, MIV
Pockets: 1 · best druggability 0.83

Structure

solution nmr · 1 distinct chain · 49% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mycinamicin IV HYDROXYLASE/EPOXIDASE (EC 1.14.-.-)	protein	393	49% helix, 12% strand	Q59523

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · chains A
MIV · Mycinamicin IV · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1112	0.83	0.84	92	HEM, MIV

Compared structures

5UHU · Solution conformation of cytochrome P450 MycG with mycinamicin IV bound · the same entry in another collection · chain A against A, TM-score 1.00
Q59523 · AlphaFold monomer V2.0 prediction for mycinamicin IV HYDROXYLASE/EPOXIDASE (Q59523) · a predicted model of the same protein · chain A against A, TM-score 0.91

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 Q59523
Elsewhere: RCSB PDB 5UHU · PDBe 5UHU · UniProt Q59523

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