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The structure of uncharacterized protein TM1266 from thermotoga maritima.

Analyse The structure of uncharacterized protein TM1266 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
2NZC
Type
protein
Length
323 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Hypothetical protein
UniProt
Q9X0Z3
Ligands
PO4
Pockets
4 · best druggability 0.77

Structure

x-ray diffraction · 3 distinct chains · 37% helix, 44% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, CHypothetical proteinprotein8039% helix, 45% strandQ9X0Z3
BHypothetical proteinprotein8137% helix, 44% strandQ9X0Z3
DHypothetical proteinprotein8237% helix, 44% strandQ9X0Z3

Ligands and binding sites

  • PO4 · Phosphate ion · ion · chains A
  • ACY · Acetic acid · additive · 4 copies · chains A, C, B, D
  • GOL · Glycerol · additive · chains A, C

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15700.770.8353PO4, ACY, GOL
24370.750.8449ACY
31750.480.7618empty
41560.450.7516empty

Interfaces

6 interfaces between chains.

  • A–B · 1104 Ų buried · 10 hydrogen bonds · protein-protein
  • C–D · 1061 Ų buried · 8 hydrogen bonds · protein-protein
  • B–D · 441 Ų buried · 15 hydrogen bonds · protein-protein
  • A–C · 400 Ų buried · 11 hydrogen bonds · protein-protein
  • B–C · 86 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 modified (engineered).

Compared structures

  • 2NZC · The structure of uncharacterized protein TM1266 from Thermotoga maritima. · the same entry in another collection · chain A against A, TM-score 1.00

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