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Crystal structure of capreomycin phosphotransferase in complex with ATP

Analyse Crystal structure of capreomycin phosphotransferase in complex with ATP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7F0B
Type
protein
Length
282 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Capreomycin phosphotransferase
UniProt
Q53826
Ligands
ATP
Pockets
3 · best druggability 0.52

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACapreomycin phosphotransferaseprotein28251% helix, 15% strandQ53826

Ligands and binding sites

  • ATP · Adenosine-5'-triphosphate · 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, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11990.520.7719ATP
2510.520.8819empty
31140.400.7618empty

Compared structures

  • 7F0B · Crystal structure of capreomycin phosphotransferase in complex with ATP · the same entry in another collection · chain A against A, TM-score 1.00

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