MolNFT v1 · #76767 · protein

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

3QUR · Foma protein: “Crystal structure of fosfomycin resistance kinase foma from streptomyces wedmorensis complexed with mgadp and…”. X-ray diffraction, 3 ligands (ADP, FM4, MG), 3 pockets (best druggability 0.48). MolNFT v1 #76767 on…

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

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q56187
Elsewhere: RCSB PDB 3QUR · PDBe 3QUR · UniProt Q56187

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