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Structure of prokaryotic transcription factors

Analyse Structure of prokaryotic transcription factors in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5NBC
Type
protein
Length
510 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ferric uptake regulation protein
UniProt
A0A0E2ZLC3
Ligands
MN, ZN
Pockets
5 · best druggability 0.85

Structure

x-ray diffraction · 4 distinct chains · 38% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AFerric uptake regulation proteinprotein13137% helix, 24% strandA0A0E2ZLC3
BFerric uptake regulation proteinprotein13038% helix, 25% strandA0A0E2ZLC3
CFerric uptake regulation proteinprotein12539% helix, 22% strandA0A0E2ZLC3
DFerric uptake regulation proteinprotein12440% helix, 23% strandA0A0E2ZLC3

Ligands and binding sites

  • MN · Manganese (II) ion · metal · 4 copies · chains A, B, C, D
  • ZN · Zinc ion · metal · 4 copies · chains A, B, C, D

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18730.850.8794empty
21380.640.8723empty
31690.640.8532empty
41560.630.8623empty
52080.570.7938empty

Interfaces

6 interfaces between chains.

  • B–C · 1550 Ų buried · 24 hydrogen bonds · protein-protein
  • A–D · 1486 Ų buried · 22 hydrogen bonds · protein-protein
  • C–D · 768 Ų buried · 7 hydrogen bonds · protein-protein
  • A–B · 652 Ų buried · 6 hydrogen bonds · protein-protein
  • A–C · 217 Ų buried · 9 hydrogen bonds · protein-protein

Compared structures

  • 5NBC · Structure of Prokaryotic Transcription Factors · the same entry in another collection · chain A against A, TM-score 1.00

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