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Structural and mechanistic insights into regulation of the retromer coat by TBC1D5

Analyse Structural and mechanistic insights into regulation of the retromer coat by… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5GTU
Type: protein
Length: 210 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Vacuolar protein sorting-associated protein 29; TBC1 domain family member 5
UniProt: Q9UBQ0, Q92609

Structure

x-ray diffraction · 2 distinct chains · 16% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Vacuolar protein sorting-associated protein 29	protein	186	15% helix, 38% strand	Q9UBQ0
B	TBC1 domain family member 5	protein	24	29% helix, 0% strand	Q92609

Interfaces

1 interface between chains.

A–B · 723 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

5GTU · Structural and mechanistic insights into regulation of the retromer coat by TBC1d5 · the same entry in another collection · chain A against A, TM-score 1.00
Q9UBQ0 · AlphaFold monomer V2.0 prediction for vacuolar protein sorting- associated protein 29… · a predicted model of the same protein · chain A against A, TM-score 0.98
Q92609 · AlphaFold monomer V2.0 prediction for TBC1 domain family member 5 (Q92609) · a predicted model of the same protein · chain B against A, TM-score 0.56

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 Q9UBQ0
Every structure of UniProt Q92609
Elsewhere: RCSB PDB 5GTU · PDBe 5GTU · UniProt Q9UBQ0 · UniProt Q92609

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