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Crystal structure of the mbth-like protein fsck bound to the interface forming region of fsch adenylation domain from thermobifida fusca

Analyse Crystal structure of the mbth-like protein fsck bound to the interface forming… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6EBY
Type
protein
Length
262 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Conserved protein mbth; Amino acid adenylation
UniProt
Q47NS3, Q47NS0
Pockets
2 · best druggability 0.59

Structure

x-ray diffraction · 2 distinct chains · 16% helix, 38% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, CConserved protein mbthprotein5426% helix, 35% strandQ47NS3
B, DAmino acid adenylationprotein779% helix, 40% strandQ47NS0

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1610.590.8917empty
2770.570.8717empty

Interfaces

3 interfaces between chains.

  • B–D · 1226 Ų buried · 15 hydrogen bonds · protein-protein
  • A–B · 931 Ų buried · 13 hydrogen bonds · protein-protein
  • C–D · 901 Ų buried · 18 hydrogen bonds · protein-protein

Compared structures

  • 6EBY · Crystal structure of the MbtH-like protein FscK bound to the interface forming region of… · the same entry in another collection · chain A against A, TM-score 1.00

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