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Crystal structure of transcription factor iib mja mini-intein

Analyse Crystal structure of transcription factor iib mja mini-intein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5O9J
Type
protein
Length
365 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Transcription initiation factor IIB,TRANSCRIPTION initiation factor iib
EC
3.1.-.-
UniProt
Q58192
Ligands
NH4
Pockets
2 · best druggability 0.60

Structure

x-ray diffraction · 2 distinct chains · 8% helix, 55% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATranscription initiation factor IIB,TRANSCRIPTION initiation factor iib (EC 3.1.-.-)protein1829% helix, 56% strandQ58192
BTranscription initiation factor IIB,TRANSCRIPTION initiation factor iib (EC 3.1.-.-)protein1837% helix, 53% strandQ58192

Ligands and binding sites

  • NH4 · Ammonium ion · ion · 10 copies · chains A, B
  • GOL · Glycerol · additive · 14 copies · chains A, B
  • DIO · 1,4-diethylene dioxide · additive · 6 copies · chains A, B
  • MES · 2-(N-morpholino)-ethanesulfonic acid · additive · chains B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12000.600.8128empty
2640.340.7617DIO, NH4

Interfaces

1 interface between chains.

  • A–B · 506 Ų buried · 4 hydrogen bonds · protein-protein

Compared structures

  • 5O9J · Crystal structure of transcription factor IIB Mja mini-intein · the same entry in another collection · chain A against A, TM-score 1.00
  • Q58192 · AlphaFold monomer V2.0 prediction for transcription initiation factor iib (Q58192) · a predicted model of the same protein · chain B against A, TM-score 0.76

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