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Crystal structure of an ABC transporter Solute Binding Protein from Klebsiella pneumoniae (KPN_01730, target EFI-511059), APO open structure

Analyse Crystal structure of an ABC transporter Solute Binding Protein from Klebsiella… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5HSG
Type
protein
Length
285 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
1.3
Source
Klebsiella pneumoniae subsp. pneumoniae
Molecule
Putative ABC transporter, nucleotide binding/ATPase protein
UniProt
A6T990
Ligands
MG
Pockets
1 · best druggability 0.54

Structure

x-ray diffraction · resolution 1.3 · 1 distinct chain · 46% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APutative ABC transporter, nucleotide binding/ATPase proteinprotein28546% helix, 20% strandA6T990

Ligands and binding sites

  • MG · Magnesium ion · metal · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12950.540.7534empty

Modifications

Observed in the structure: 5 modified (engineered).

Compared structures

  • 5HSG · Crystal structure of an ABC transporter solute binding protein from klebsiella pneumoniae… · the same entry in another collection · chain A against A, TM-score 1.00

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