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

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: 3D41
Type: protein
Length: 268 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Foma protein
UniProt: Q56187
Ligands: ANP, FCN, MG
Pockets: 2 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Foma protein	protein	268	37% helix, 22% strand	Q56187

Ligands and binding sites

ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · chains A
FCN · Fosfomycin · 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

2 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	233	0.69	0.86	43	MG, ANP, FCN
2	64	0.50	0.86	17	empty

Compared structures

3D41 · 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 3D41 · PDBe 3D41 · UniProt Q56187

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