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The crystal structure of premithramycin B in complex with mtmoiv, a baeyer-villiger monooxygenase from the mithramycin biosynthetic pathway in streptomyces argillaceus.

Analyse The crystal structure of premithramycin B in complex with mtmoiv, a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4K5S
Type: protein
Length: 490 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Oxygenase
UniProt: Q194P4
Ligands: FAD, PM0
Pockets: 5 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Oxygenase	protein	490	34% helix, 28% strand	Q194P4

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · chains A
PM0 · premithramycin B · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1093	0.79	0.81	97	FAD, PM0
2	101	0.56	0.85	26	empty
3	58	0.45	0.84	19	empty
4	111	0.45	0.78	22	empty
5	72	0.37	0.78	21	empty

Compared structures

4K5S · The crystal structure of premithramycin B in complex with MTMOIV, a baeyer-villiger… · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q194P4
Elsewhere: RCSB PDB 4K5S · PDBe 4K5S · UniProt Q194P4

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