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MolNFT v1 · #145998 · protein

Crystal structure of a Fc fragment of rhesus macaque (macaca mulatta) IGG1.

6D4E · Fc fragment of IGG1: “Crystal structure of a Fc fragment of rhesus macaque (macaca mulatta) IGG1.”. X-ray diffraction, 5 ligands (NAG, MAN, BMA), 3 pockets (best druggability 0.34). MolNFT v1 #145998 on GenesisL1: 3D structure…

PDB
6D4E
Type
protein
Length
418 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Fc fragment of IGG1
UniProt
F6RL33
Ligands
NAG, MAN, BMA, FUC, CL
Pockets
3 · best druggability 0.34

Structure

x-ray diffraction · 2 distinct chains · 10% helix, 47% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AFc fragment of IGG1protein20810% helix, 48% strandF6RL33
BFc fragment of IGG1protein21010% helix, 45% strandF6RL33

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 8 copies · chains A, B
  • MAN · alpha-D-mannopyranose · sugar · 4 copies · chains A, B
  • BMA · beta-D-mannopyranose · sugar · 2 copies · chains A, B
  • FUC · alpha-L-fucopyranose · sugar · 2 copies
  • CL · Chloride ion · ion · chains A

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

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1970.340.7322empty
2550.300.7615empty
3510.280.7513empty

Interfaces

1 interface between chains.

  • A–B · 1155 Ų buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide, 2 glycan (disulfide, N-glycosylation).

Compared structures

  • 6D4E · Crystal Structure of a Fc Fragment of Rhesus macaque (Macaca mulatta) IgG1. · the same entry in another collection · chain A against A, TM-score 1.00

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