GL1X · GenesisL1 explorer

Research workbench

Crystal structure of uncharacterized conserved protein from thermotoga maritima

Analyse Crystal structure of uncharacterized conserved protein from thermotoga maritima in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2ZBV
Type
protein
Length
781 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Uncharacterized conserved protein
UniProt
Q9WZC8
Ligands
ADN
Pockets
13 · best druggability 0.82

Structure

x-ray diffraction · 3 distinct chains · 25% helix, 30% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AUncharacterized conserved proteinprotein26325% helix, 30% strandQ9WZC8
BUncharacterized conserved proteinprotein25824% helix, 30% strandQ9WZC8
CUncharacterized conserved proteinprotein26024% helix, 30% strandQ9WZC8

Ligands and binding sites

  • ADN · Adenosine · ligand · 3 copies · chains A, B, C

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

Pockets

13 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11760.820.9740ADN
24180.820.9047empty
31510.810.9730ADN
41310.800.9726ADN
51390.520.8023empty

Interfaces

3 interfaces between chains.

  • A–B · 1329 Ų buried · 12 hydrogen bonds · protein-protein
  • A–C · 1312 Ų buried · 9 hydrogen bonds · protein-protein
  • B–C · 1300 Ų buried · 13 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 modified (engineered).

Compared structures

  • 2ZBV · Crystal structure of uncharacterized conserved protein from Thermotoga maritima · 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.