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Crystal structure of the TCERG1 FF4-6 tandem repeat domain

Analyse Crystal structure of the TCERG1 FF4-6 tandem repeat domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4FQG
Type
protein
Length
375 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Transcription elongation regulator 1
UniProt
O14776
Ligands
NI, CL
Pockets
2 · best druggability 0.43

Structure

x-ray diffraction · 2 distinct chains · 72% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATranscription elongation regulator 1protein18673% helix, 0% strandO14776
BTranscription elongation regulator 1protein18972% helix, 0% strandO14776

Ligands and binding sites

  • NI · Nickel (II) ion · metal · 2 copies · chains A, B
  • CL · Chloride ion · ion · 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, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11590.430.7422empty
2740.290.7216empty

Interfaces

1 interface between chains.

  • A–B · 205 Ų buried · 2 hydrogen bonds · protein-protein

Compared structures

  • 4FQG · Crystal structure of the TCERG1 FF4-6 tandem repeat domain · the same entry in another collection · chain A against A, TM-score 1.00
  • O14776 · AlphaFold monomer V2.0 prediction for transcription elongation regulator 1 (O14776) · a predicted model of the same protein · chain A against A, TM-score 0.91

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