MolNFT v1 · #180730 · protein

Crystal structure of apo-alpha glucosidase

7L9E: “Crystal structure of apo-alpha glucosidase”. X-ray diffraction, 2 ligands (CA, SO4). MolNFT v1 #180730 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7L9E
Type: protein
Length: 1,878 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q8BHN3, O08795
Ligands: CA, SO4

Structure

x-ray diffraction · 7 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
E	—	protein	150	—	Q8BHN3
F	—	protein	105	—	Q8BHN3
A, C	—	protein	597	—	Q8BHN3
B	—	protein	85	—	O08795
G	—	protein	153	—	Q8BHN3
H	—	protein	107	—	Q8BHN3
D	—	protein	84	—	O08795

Ligands and binding sites

CA · Calcium ion · metal · 4 copies · chains B, D
SO4 · Sulfate ion · ion · 3 copies · chains A, C
EDO · 1,2-ethanediol · additive · 23 copies · chains E, A, F, B, G, H, C, D
PEG · Di(hydroxyethyl)ether · additive · 3 copies · chains A, B
PG4 · Tetraethylene glycol · additive · chains A

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

Compared structures

7L9E · Crystal structure of apo-alpha glucosidase · the same entry in another collection · chain D against D, TM-score 1.00
Q8BHN3 · AlphaFold monomer V2.0 prediction for neutral alpha-glucosidase ab (Q8BHN3) · a predicted model of the same protein · chain A against A, 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
Every structure of UniProt Q8BHN3
Every structure of UniProt O08795
Elsewhere: RCSB PDB 7L9E · PDBe 7L9E · UniProt Q8BHN3 · UniProt O08795

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