Research workbench

TDRD3 complex

Analyse TDRD3 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2LTO
Type: protein
Length: 71 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tudor domain-containing protein 3; DNA-directed RNA polymerase II subunit RPB1
EC: 2.7.7.6, 2.7.7.48
UniProt: Q9H7E2, P24928

Structure

solution nmr · 2 distinct chains · 4% helix, 38% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tudor domain-containing protein 3	protein	58	5% helix, 47% strand	Q9H7E2
B	DNA-directed RNA polymerase II subunit RPB1 (EC 2.7.7.6, 2.7.7.48)	protein	13	0% helix, 0% strand	P24928

Interfaces

1 interface between chains.

A–B · 295 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (nonstandard).

Compared structures

2LTO · TDRD3 complex · the same entry in another collection · chain A against A, TM-score 1.00
Q9H7E2 · AlphaFold monomer V2.0 prediction for tudor domain-containing protein 3 (Q9H7E2) · a predicted model of the same protein · chain A against A, TM-score 0.83
P24928 · AlphaFold monomer V2.0 prediction for DNA-directed RNA polymerase II subunit RPB1 (P24928) · a predicted model of the same protein · chain B against A, TM-score 0.30

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 Q9H7E2
Every structure of UniProt P24928
Elsewhere: RCSB PDB 2LTO · PDBe 2LTO · UniProt Q9H7E2 · UniProt P24928

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