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Crystal structure of a monomeric SCP2-thiolase like protein type 1 (STLP1) from mycobacterium smegmatis

Analyse Crystal structure of a monomeric SCP2-thiolase like protein type 1 (STLP1) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4EGV
Type
protein
Length
2,694 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Acetyl-CoA acetyltransferase
UniProt
A0R3M0
Pockets
20 · best druggability 0.70

Structure

x-ray diffraction · 6 distinct chains · 37% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAcetyl-CoA acetyltransferaseprotein44838% helix, 24% strandA0R3M0
BAcetyl-CoA acetyltransferaseprotein45238% helix, 24% strandA0R3M0
CAcetyl-CoA acetyltransferaseprotein45337% helix, 24% strandA0R3M0
DAcetyl-CoA acetyltransferaseprotein44538% helix, 25% strandA0R3M0
EAcetyl-CoA acetyltransferaseprotein44736% helix, 25% strandA0R3M0
FAcetyl-CoA acetyltransferaseprotein44937% helix, 25% strandA0R3M0

Pockets

20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19050.700.7593empty
27630.670.7590empty
35650.660.7677empty
43350.630.7942empty
53660.620.7849empty

Interfaces

11 interfaces between chains.

  • E–F · 723 Ų buried · 12 hydrogen bonds · protein-protein
  • A–B · 680 Ų buried · 6 hydrogen bonds · protein-protein
  • B–C · 646 Ų buried · 5 hydrogen bonds · protein-protein
  • D–E · 618 Ų buried · 4 hydrogen bonds · protein-protein
  • D–F · 610 Ų buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 58 modified (engineered).

Compared structures

  • 4EGV · Crystal structure of a monomeric SCP2-thiolase like protein type 1 (STLP1) from… · the same entry in another collection · chain E against E, TM-score 1.00

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