MolNFT v1 · #170218 · protein

Structure of human fapalpha in complex with linagliptin

6Y0F: “Structure of human fapalpha in complex with linagliptin”. X-ray diffraction, 4 ligands (356, NAG, FUC). MolNFT v1 #170218 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6Y0F
Type: protein
Length: 2,882 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q12884
Ligands: 356, NAG, FUC, BMA

Structure

x-ray diffraction · 4 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	721	—	Q12884
B	—	protein	719	—	Q12884
C	—	protein	722	—	Q12884
D	—	protein	720	—	Q12884

Ligands and binding sites

356 · 8-[(3R)-3-Aminopiperidin-1-yl]-7-but-2-yn-1-yl-3-methyl-1-[(4-methylquinazolin-2-yl)methyl]-3,7-dihydro-1H-purine-2,6-d ione · ligand · 4 copies · chains A, B, C, D
NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 21 copies · chains A, B, D, C
FUC · alpha-L-fucopyranose · sugar · 3 copies · chains D
BMA · beta-D-mannopyranose · sugar

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

Compared structures

6Y0F · Structure of human FAPalpha in complex with linagliptin · the same entry in another collection · chain D against D, TM-score 1.00
Q12884 · AlphaFold monomer V2.0 prediction for prolyl endopeptidase fap (Q12884) · a predicted model of the same protein · chain D 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 Q12884
Elsewhere: RCSB PDB 6Y0F · PDBe 6Y0F · UniProt Q12884

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