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Crystal structure of C-terminal variant 1 of chaetomium thermophilum acetyl-CoA carboxylase

Analyse Crystal structure of C-terminal variant 1 of chaetomium thermophilum acetyl-CoA… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5I6F
Type
protein
Length
2,092 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Acetyl-CoA carboxylase-like protein
UniProt
G0S3L5
Pockets
20 · best druggability 0.85

Structure

x-ray diffraction · 2 distinct chains · 36% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAcetyl-CoA carboxylase-like proteinprotein104436% helix, 19% strandG0S3L5
BAcetyl-CoA carboxylase-like proteinprotein104836% helix, 20% strandG0S3L5

Pockets

20 pockets found on a 1 Å grid, 17 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13590.850.9434empty
29220.830.8561empty
33080.800.9147empty
43040.770.8841empty
53840.730.8449empty

Interfaces

1 interface between chains.

  • A–B · 7153 Ų buried · 54 hydrogen bonds · protein-protein

Compared structures

  • 5I6F · Crystal structure of C-terminal variant 1 of Chaetomium thermophilum acetyl-CoA… · the same entry in another collection · chain A against A, TM-score 1.00

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