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Crystal structure of TTHMTA1-PTEMTA9 complex

Analyse Crystal structure of TTHMTA1-PTEMTA9 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7F4S
Type
protein
Length
1,152 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Mt-A70 family protein; MTA9
UniProt
Q22GC0, A0E887
Pockets
20 · best druggability 0.80

Structure

x-ray diffraction · 6 distinct chains · 22% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMt-A70 family proteinprotein17822% helix, 22% strandQ22GC0
BMt-A70 family proteinprotein17822% helix, 20% strandQ22GC0
CMt-A70 family proteinprotein17625% helix, 22% strandQ22GC0
DMTA9protein21519% helix, 26% strandA0E887
EMTA9protein21321% helix, 15% strandA0E887
FMTA9protein19223% helix, 16% strandA0E887

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17570.800.8371empty
28810.790.8274empty
311300.790.81108empty
4620.690.9619empty
52240.670.8432empty

Interfaces

7 interfaces between chains.

  • C–E · 1818 Ų buried · 32 hydrogen bonds · protein-protein
  • A–D · 1608 Ų buried · 16 hydrogen bonds · protein-protein
  • B–F · 1600 Ų buried · 18 hydrogen bonds · protein-protein
  • A–B · 626 Ų buried · 2 hydrogen bonds · protein-protein
  • A–C · 466 Ų buried · 1 hydrogen bond · protein-protein

Compared structures

  • 7F4S · Crystal structure of TthMTA1-PteMTA9 complex · the same entry in another collection · chain A against A, TM-score 1.00

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