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Crystal structure of amycolatopsis cytochrome P450 gcoa in complex with syringol

Analyse Crystal structure of amycolatopsis cytochrome P450 gcoa in complex with syringol in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5OMU
Type: protein
Length: 402 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytochrome P450
UniProt: A0A076MY51
Ligands: HEM, 3DM
Pockets: 3 · best druggability 0.86

Structure

x-ray diffraction · 1 distinct chain · 57% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cytochrome P450	protein	402	57% helix, 10% strand	A0A076MY51

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · chains A
3DM · 2,6-dimethoxyphenol · 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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	384	0.86	0.94	44	HEM, 3DM
2	99	0.41	0.77	16	empty
3	58	0.32	0.76	13	empty

Compared structures

5OMU · Crystal structure of Amycolatopsis cytochrome P450 GcoA in complex with syringol · the same entry in another collection · chain A against A, TM-score 1.00

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 A0A076MY51
Elsewhere: RCSB PDB 5OMU · PDBe 5OMU · UniProt A0A076MY51

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