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Crystal structure of semet arg R 1

Analyse Crystal structure of semet arg R 1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2X46
Type: protein
Length: 144 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Allergen arg R 1
UniProt: Q5GQ85
Pockets: 1 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 13% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Allergen arg R 1	protein	144	13% helix, 40% strand	Q5GQ85

Ligands and binding sites

TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	211	0.68	0.85	36	TRS

Modifications

Observed in the structure: 3 disulfide, 3 modified (disulfide, engineered).

Compared structures

2X46 · Crystal Structure of SeMet Arg r 1 · the same entry in another collection · chain A against A, TM-score 1.00
Q5GQ85 · AlphaFold monomer V2.0 prediction for allergen arg R 1 (Q5GQ85) · 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 Q5GQ85
Elsewhere: RCSB PDB 2X46 · PDBe 2X46 · UniProt Q5GQ85

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