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MolNFT v1 · #114310 · protein

Crystal structure of human fcrn with a peptide inhibitor at multiple sites

5BJT · IgG receptor fcrn large subunit P51: “Crystal structure of human fcrn with a peptide inhibitor at multiple sites”. X-ray diffraction, 20 pockets (best druggability 0.76). MolNFT v1 #114310 on GenesisL1: 3D structure, binding sites…

PDB
5BJT
Type
protein
Length
1,560 residues
Chains
15
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
IgG receptor fcrn large subunit P51; Beta-2-microglobulin; Peptide inhibitor
UniProt
P55899, P61769
Pockets
20 · best druggability 0.76

Structure

x-ray diffraction · 3 distinct chains · 17% helix, 42% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, C, E, GIgG receptor fcrn large subunit P51protein26324% helix, 41% strandP55899
B, D, F, HBeta-2-microglobulinprotein990% helix, 49% strandP61769
P, Q, R, S, T, U, VPeptide inhibitorprotein160% helix, 6% strand—

Pockets

20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111100.760.79105empty
26110.720.8061empty
36590.670.7658empty
45040.650.7755empty
54420.630.7748empty

Interfaces

30 interfaces between chains.

  • E–F · 1375 Ų buried · 22 hydrogen bonds · protein-protein
  • C–D · 1371 Ų buried · 19 hydrogen bonds · protein-protein
  • A–B · 1343 Ų buried · 15 hydrogen bonds · protein-protein
  • G–H · 1209 Ų buried · 13 hydrogen bonds · protein-protein
  • E–R · 505 Ų buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 18 disulfide (disulfide).

Compared structures

  • 5BJT · Crystal structure of human FcRn with a peptide inhibitor at multiple sites · the same entry in another collection · chain V against V, TM-score 1.00

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