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Crystal structure of the C-terminal mu homology domain of SYP1

Analyse Crystal structure of the C-terminal mu homology domain of SYP1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3G9H
Type: protein
Length: 262 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Suppressor of yeast profilin deletion
UniProt: P25623
Ligands: 1PG
Pockets: 1 · best druggability 0.30

Structure

x-ray diffraction · 1 distinct chain · 1% helix, 58% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Suppressor of yeast profilin deletion	protein	262	1% helix, 58% strand	P25623

Ligands and binding sites

1PG · 2-(2-{2-[2-(2-methoxy-ethoxy)-ethoxy]-ethoxy}-ethoxy)-ethanol · ligand · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	58	0.30	0.75	14	empty

Compared structures

3G9H · Crystal structure of the C-terminal mu homology domain of Syp1 · the same entry in another collection · chain A against A, TM-score 1.00
P25623 · AlphaFold monomer V2.0 prediction for suppressor of yeast profilin deletion (P25623) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P25623
Elsewhere: RCSB PDB 3G9H · PDBe 3G9H · UniProt P25623

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