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2.2 ångström crystal structure of ABC transporter substrate binding protein ctap (LMO0135) from listeria monocytogenes.

Analyse 2.2 ångström crystal structure of ABC transporter substrate binding protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5ISU
Type
protein
Length
488 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
LMO0135 protein
UniProt
Q8YAJ0
Pockets
2 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ALMO0135 proteinprotein48833% helix, 25% strandQ8YAJ0

Ligands and binding sites

  • EDO · 1,2-ethanediol · additive · 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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17520.730.7966empty
25190.650.7757empty

Compared structures

  • 5ISU · 2.2 Angstrom Crystal Structure of ABC Transporter Substrate Binding Protein CtaP… · the same entry in another collection · chain A against A, TM-score 1.00

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