MolNFT v1 · #39421 · protein

Structural basis for ubiquitin recognition by the human EAP45/ESCRT-II glue domain

2HTH: “Structural basis for ubiquitin recognition by the human EAP45/ESCRT-II glue domain”. X-ray diffraction, 2 pockets (best druggability 0.51). MolNFT v1 #39421 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2HTH
Type: protein
Length: 202 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ubiquitin; Vacuolar protein sorting protein 36
UniProt: P62988, Q86VN1
Pockets: 2 · best druggability 0.51

Structure

x-ray diffraction · 2 distinct chains · 16% helix, 37% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ubiquitin	protein	73	21% helix, 34% strand	P62988
B	Vacuolar protein sorting protein 36	protein	129	13% helix, 38% strand	Q86VN1

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	177	0.51	0.78	22	empty
2	93	0.36	0.75	17	empty

Interfaces

1 interface between chains.

A–B · 521 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

2HTH · Structural basis for ubiquitin recognition by the human EAP45/ESCRT-II GLUE domain · the same entry in another collection · chain A against A, TM-score 1.00
Q86VN1 · AlphaFold monomer V2.0 prediction for vacuolar protein-sorting- associated protein 36… · a predicted model of the same protein · chain B against A, TM-score 0.85

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 P62988
Every structure of UniProt Q86VN1
Elsewhere: RCSB PDB 2HTH · PDBe 2HTH · UniProt P62988 · UniProt Q86VN1

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