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Hyperlytic variant of TAE1, type VI secretion amidase effector 1, from pseudomonas aeruginosa (CYS110SER)

Analyse Hyperlytic variant of TAE1, type VI secretion amidase effector 1, from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7TVH
Type
protein
Length
584 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Peptidoglycan amidase TSE1
EC
3.4.19.11
UniProt
Q9I2Q1
Pockets
4 · best druggability 0.67

Structure

x-ray diffraction · 3 distinct chains · 38% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APeptidoglycan amidase TSE1 (EC 3.4.19.11)protein14538% helix, 21% strandQ9I2Q1
B, DPeptidoglycan amidase TSE1 (EC 3.4.19.11)protein14638% helix, 21% strandQ9I2Q1
CPeptidoglycan amidase TSE1 (EC 3.4.19.11)protein14738% helix, 20% strandQ9I2Q1

Pockets

4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17460.670.7588empty
2790.530.8527empty
3790.510.8429empty
4780.280.7217empty

Interfaces

5 interfaces between chains.

  • A–B · 694 Ų buried · 6 hydrogen bonds · protein-protein
  • C–D · 689 Ų buried · 6 hydrogen bonds · protein-protein
  • A–D · 381 Ų buried · 5 hydrogen bonds · protein-protein
  • B–C · 370 Ų buried · 4 hydrogen bonds · protein-protein
  • A–C · 50 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

  • 7TVH · Hyperlytic variant of Tae1, Type VI secretion amidase effector 1, from Pseudomonas… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9I2Q1 · AlphaFold monomer V2.0 prediction for peptidoglycan amidase TSE1 (Q9I2Q1) · a predicted model of the same protein · chain B against A, TM-score 0.99

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