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Structure of escherichia COLI RNA polymerase alpha subunit N-terminal domain

Analyse Structure of escherichia COLI RNA polymerase alpha subunit N-terminal domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1BDF
Type
protein
Length
917 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
RNA polymerase alpha subunit
EC
2.7.7.6
UniProt
P0A7Z4
Pockets
9 · best druggability 0.79

Structure

x-ray diffraction · 4 distinct chains · 20% helix, 36% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARNA polymerase alpha subunit (EC 2.7.7.6)protein22621% helix, 36% strandP0A7Z4
BRNA polymerase alpha subunit (EC 2.7.7.6)protein23220% helix, 38% strandP0A7Z4
CRNA polymerase alpha subunit (EC 2.7.7.6)protein22819% helix, 34% strandP0A7Z4
DRNA polymerase alpha subunit (EC 2.7.7.6)protein23119% helix, 35% strandP0A7Z4

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18390.790.82110empty
2660.680.9517empty
33370.540.7426empty
42880.520.7432empty
51440.480.7821empty

Interfaces

5 interfaces between chains.

  • C–D · 1856 Ų buried · 16 hydrogen bonds · protein-protein
  • A–B · 1814 Ų buried · 15 hydrogen bonds · protein-protein
  • B–C · 1038 Ų buried · 13 hydrogen bonds · protein-protein
  • B–D · 102 Ų buried · 2 hydrogen bonds · protein-protein
  • A–C · 68 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 1BDF · Structure of escherichia COLI RNA polymerase alpha subunit N-terminal domain · the same entry in another collection · chain A against A, TM-score 1.00

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