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Crystal structure of a methyl-accepting chemotaxis protein, residues 122 to 287

Analyse Crystal structure of a methyl-accepting chemotaxis protein, residues 122 to 287 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3OOV
Type
protein
Length
326 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Methyl-accepting chemotaxis protein, putative
UniProt
Q74CG9
Pockets
1 · best druggability 0.65

Structure

x-ray diffraction · 2 distinct chains · 44% helix, 23% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMethyl-accepting chemotaxis protein, putativeprotein16443% helix, 23% strandQ74CG9
BMethyl-accepting chemotaxis protein, putativeprotein16244% helix, 23% strandQ74CG9

Ligands and binding sites

  • GOL · Glycerol · additive · 4 copies · chains A, B

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
13670.650.7953GOL

Interfaces

1 interface between chains.

  • A–B · 700 Ų buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (engineered).

Compared structures

  • 3OOV · Crystal structure of a methyl-accepting chemotaxis protein, residues 122 to 287 · the same entry in another collection · chain A against A, TM-score 1.00

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