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Crystal structure of fosfomycin resistance kinase foma from streptomyces wedmorensis complexed with mgadp and fosfomycin monophosphate

Analyse Crystal structure of fosfomycin resistance kinase foma from streptomyces… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3QUR
Type: protein
Length: 249 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Foma protein
UniProt: Q56187
Ligands: ADP, FM4, MG
Pockets: 3 · best druggability 0.48

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Foma protein	protein	249	37% helix, 27% strand	Q56187

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · chains A
FM4 · [(2R,3S)-3-methyloxiran-2-yl]-phosphonooxy-phosphinic acid · ligand · chains A
MG · Magnesium ion · metal · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	66	0.48	0.84	16	empty
2	130	0.37	0.73	34	FM4, MG
3	54	0.34	0.78	14	empty

Compared structures

3QUR · Crystal structure of fosfomycin resistance kinase FomA from Streptomyces wedmorensis… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

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Every structure of UniProt Q56187
Elsewhere: RCSB PDB 3QUR · PDBe 3QUR · UniProt Q56187

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