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Crystal structure of TT1020 from thermus thermophilus HB8

Analyse Crystal structure of TT1020 from thermus thermophilus HB8 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1UFL
Type
protein
Length
303 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Nitrogen regulatory protein P-II
UniProt
P83820
Pockets
6 · best druggability 0.67

Structure

x-ray diffraction · 3 distinct chains · 27% helix, 39% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ANitrogen regulatory protein P-IIprotein10823% helix, 45% strandP83820
BNitrogen regulatory protein P-IIprotein9633% helix, 36% strandP83820
CNitrogen regulatory protein P-IIprotein9924% helix, 34% strandP83820

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11890.670.8636empty
21340.550.8220empty
31950.520.7829empty
4510.480.8620empty
5600.380.8015empty

Interfaces

3 interfaces between chains.

  • A–B · 1201 Ų buried · 12 hydrogen bonds · protein-protein
  • B–C · 1127 Ų buried · 14 hydrogen bonds · protein-protein
  • A–C · 1110 Ų buried · 18 hydrogen bonds · protein-protein

Compared structures

  • 1UFL · Crystal Structure of TT1020 from Thermus thermophilus HB8 · the same entry in another collection · chain A against A, TM-score 1.00

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