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Crystal structure of a yeast BRF1-tbp-DNA ternary complex

Analyse Crystal structure of a yeast BRF1-tbp-DNA ternary complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1NGM
Type
protein + DNA
Length
1,122 residues
Chains
16
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
5'- D(*CP*TP*AP*TP*AP*AP*AP*AP*AP*AP*AP*TP*GP*TP*TP*TP*TP*TP*T) -3'; 5'…
UniProt
P13393, P29056
Pockets
11 · best druggability 0.71

Structure

x-ray diffraction · 5 distinct chains · 33% helix, 13% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
C, G, K, O5'- D(*CP*TP*AP*TP*AP*AP*AP*AP*AP*AP*AP*TP*GP*TP*TP*TP*TP*TP*T) -3'dna19——
D, H, L, P5'- D(*AP*AP*AP*AP*AP*AP*CP*AP*TP*TP*TP*TP*TP*TP*TP*AP*TP*AP*G) -3'dna19——
A, E, I, MTranscription initiation factor tfiidprotein18022% helix, 22% strandP13393
B, FTranscription factor iiib BRF1 subunitprotein7244% helix, 0% strandP29056
J, NTranscription factor iiib BRF1 subunitprotein5357% helix, 0% strandP29056

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15530.710.8065empty
21650.500.7825empty
31800.490.7730empty
41830.480.7628empty
5930.370.7518empty

Interfaces

31 interfaces between chains.

  • A–B · 1996 Ų buried · 32 hydrogen bonds · protein-protein
  • E–F · 1940 Ų buried · 35 hydrogen bonds · protein-protein
  • M–N · 1517 Ų buried · 28 hydrogen bonds · protein-protein
  • I–J · 1488 Ų buried · 29 hydrogen bonds · protein-protein
  • D–A · 870 Ų buried · 9 hydrogen bonds · protein-nucleic

Compared structures

  • 1NGM · Crystal structure of a yeast Brf1-TBP-DNA ternary complex · the same entry in another collection · chain N against N, TM-score 1.00

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