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Structure of the tpr oligomerization domain

Analyse Structure of the tpr oligomerization domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5TVB
Type: protein
Length: 280 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nucleoprotein tpr
UniProt: P12270

Structure

x-ray diffraction · 1 distinct chain · 93% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Nucleoprotein tpr	protein	140	93% helix, 0% strand	P12270

Interfaces

1 interface between chains.

A–B · 3708 Å² buried · 18 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 modified (engineered).

Compared structures

5TVB · Structure of the TPR oligomerization domain · the same entry in another collection · chain A against A, TM-score 1.00
P12270 · AlphaFold monomer V2.0 prediction for nucleoprotein tpr (P12270) · a predicted model of the same protein · chain A against A, TM-score 0.73

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 P12270
Elsewhere: RCSB PDB 5TVB · PDBe 5TVB · UniProt P12270

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