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Crystal structure of the tetrahymena telomerase processivity factor TEB1 ob-B

Analyse Crystal structure of the tetrahymena telomerase processivity factor TEB1 ob-B in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3U4Z
Type: protein
Length: 218 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Telomerase-associated protein 82
UniProt: D2CVN6
Pockets: 3 · best druggability 0.35

Structure

x-ray diffraction · 1 distinct chain · 11% helix, 39% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Telomerase-associated protein 82	protein	109	11% helix, 39% strand	D2CVN6

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	96	0.35	0.74	17	empty
2	91	0.32	0.73	16	empty
3	54	0.27	0.74	13	empty

Interfaces

1 interface between chains.

A–B · 689 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

3U4Z · Crystal Structure of the Tetrahymena telomerase processivity factor Teb1 OB-B · the same entry in another collection · chain A against A, TM-score 1.00
D2CVN6 · AlphaFold monomer V2.0 prediction for telomeric repeat-binding subunit 1 (D2CVN6) · a predicted model of the same protein · chain A against A, TM-score 0.87

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 D2CVN6
Elsewhere: RCSB PDB 3U4Z · PDBe 3U4Z · UniProt D2CVN6

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