GL1X · GenesisL1 explorer

Research workbench

Crystal structure of hydrogenase 2 maturation peptidase from thaumarchaeota archaeon SCGC_AB-539-E09

Analyse Crystal structure of hydrogenase 2 maturation peptidase from thaumarchaeota… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5TTX
Type
protein
Length
612 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Hydrogenase 2 maturation peptidase
UniProt
M7TUZ8
Pockets
3 · best druggability 0.53

Structure

x-ray diffraction · 3 distinct chains · 39% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BHydrogenase 2 maturation peptidaseprotein15438% helix, 24% strandM7TUZ8
CHydrogenase 2 maturation peptidaseprotein15140% helix, 25% strandM7TUZ8
DHydrogenase 2 maturation peptidaseprotein15339% helix, 25% strandM7TUZ8

Ligands and binding sites

  • GOL · Glycerol · additive · chains A, D

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11820.530.7826empty
2790.350.7619empty
3610.300.7415empty

Interfaces

3 interfaces between chains.

  • A–D · 1559 Ų buried · 26 hydrogen bonds · protein-protein
  • B–C · 1423 Ų buried · 18 hydrogen bonds · protein-protein
  • A–B · 442 Ų buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 modified (engineered).

Compared structures

  • 5TTX · Crystal structure of hydrogenase 2 maturation peptidase from Thaumarchaeota archaeon… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.