Research workbench

Crystal structure of human alr mutant C142/145S

Analyse Crystal structure of human alr mutant C142/145S in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3U2M
Type: protein
Length: 115 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: FAD-linked sulfhydryl oxidase alr
EC: 1.8.3.2
UniProt: P55789
Ligands: FAD
Pockets: 1 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 65% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	FAD-linked sulfhydryl oxidase alr (EC 1.8.3.2)	protein	115	65% helix, 0% strand	P55789

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	197	0.63	0.83	27	FAD

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

3U2M · Crystal structure of human ALR mutant C142/145S · the same entry in another collection · chain A against A, TM-score 1.00
P55789 · AlphaFold monomer V2.0 prediction for FAD-linked sulfhydryl oxidase alr (P55789) · 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 P55789
Elsewhere: RCSB PDB 3U2M · PDBe 3U2M · UniProt P55789

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.