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Crystal structure of yeast tata-binding protein and model for interaction with DNA

Analyse Crystal structure of yeast tata-binding protein and model for interaction with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1TBP
Type: protein
Length: 360 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tata-binding protein
UniProt: P13393
Pockets: 3 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 25% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Tata-binding protein	protein	180	25% helix, 33% strand	P13393

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	198	0.59	0.81	37	empty
2	201	0.52	0.77	37	empty
3	70	0.30	0.73	17	empty

Interfaces

1 interface between chains.

A–B · 1445 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

1TBP · Crystal structure of yeast tata-binding protein and model for interaction with DNA · the same entry in another collection · chain A against A, TM-score 1.00
P13393 · AlphaFold monomer V2.0 prediction for tata-box-binding protein (P13393) · a predicted model of the same protein · chain A against A, TM-score 0.94

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P13393
Elsewhere: RCSB PDB 1TBP · PDBe 1TBP · UniProt P13393

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