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An oligomeric domain-swapped beta-beta-alpha mini-protein

Analyse An oligomeric domain-swapped beta-beta-alpha mini-protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1SNE
Type: protein
Length: 42 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tetrameric beta-beta-alpha mini-protein
Ligands: ACE, NH2
Pockets: 1 · best druggability 0.26

Structure

x-ray diffraction · 1 distinct chain · 62% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Tetrameric beta-beta-alpha mini-protein	protein	21	62% helix, 19% strand	—

Ligands and binding sites

ACE · Acetyl group · ligand · 2 copies · chains A, B
NH2 · Amino group · ion · 2 copies · chains A, B
IPA · Isopropyl alcohol · additive · 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	57	0.26	0.73	10	empty

Interfaces

1 interface between chains.

A–B · 266 Å² buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 4 d-amino, 4 modified, 2 covalent (D-amino acid, nonstandard, covalent ligand).

Compared structures

1SNE · An Oligomeric Domain-Swapped Beta-Beta-Alpha Mini-Protein · the same entry in another collection · chain B against B, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Elsewhere: RCSB PDB 1SNE · PDBe 1SNE

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