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Crystal structure of acinetobacter baumannii CARO1

Analyse Crystal structure of acinetobacter baumannii CARO1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4RL9
Type
protein
Length
409 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Carbapenem-associated resistance protein
UniProt
A6XB80
Pockets
4 · best druggability 0.49

Structure

x-ray diffraction · 2 distinct chains · 10% helix, 66% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACarbapenem-associated resistance proteinprotein20511% helix, 64% strandA6XB80
BCarbapenem-associated resistance proteinprotein2049% helix, 67% strandA6XB80

Pockets

4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11440.490.7826empty
21620.480.7629empty
31650.450.7525empty
4510.420.8318empty

Interfaces

1 interface between chains.

  • A–B · 285 Ų buried · 1 hydrogen bond · protein-protein

Compared structures

  • 4RL9 · Crystal structure of Acinetobacter baumannii CarO1 · the same entry in another collection · chain A against A, TM-score 1.00

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