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MolNFT v1 · #19925 · protein

Crystal structure of N-terminal domain of human platelet receptor glycoprotein ib-alpha at 2.8 ångström resolution

1QYY · Platelet glycoprotein ib alpha chain: “Crystal structure of N-terminal domain of human platelet receptor glycoprotein ib-alpha at 2.8 ångström…”. X-ray diffraction, 3 ligands (NAG, MAN, PT), 5 pockets (best druggability 0.71).…

PDB
1QYY
Type
protein
Length
532 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Platelet glycoprotein ib alpha chain
UniProt
P07359
Ligands
NAG, MAN, PT
Pockets
5 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 11% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, GPlatelet glycoprotein ib alpha chainprotein26611% helix, 15% strandP07359

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A, G
  • MAN · alpha-D-mannopyranose · sugar · 2 copies
  • PT · Platinum (II) ion · metal · 3 copies · chains A, G

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

Pockets

5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12960.710.8540PT
21770.650.8525empty
31510.450.7622empty
41520.440.7530empty
5830.420.7915empty

Interfaces

1 interface between chains.

  • A–G · 812 Ų buried · 15 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide, 2 glycan (disulfide, N-glycosylation).

Compared structures

  • 1QYY · Crystal Structure of N-Terminal Domain of Human Platelet Receptor Glycoprotein Ib-alpha… · the same entry in another collection · chain A against A, TM-score 1.00
  • P07359 · AlphaFold monomer V2.0 prediction for platelet glycoprotein ib alpha chain (P07359) · a predicted model of the same protein · chain A against A, TM-score 0.97

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