Research workbench
Crystal structure of human fcrn with a monomeric peptide inhibitor
Analyse Crystal structure of human fcrn with a monomeric peptide inhibitor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3M17
- Type
- protein
- Length
- 1,500 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- IgG receptor fcrn large subunit P51; Beta-2-microglobulin; Monomeric peptide inhibitor
- UniProt
- P55899, P61769
- Ligands
- ACE, NH2
- Pockets
- 12 · best druggability 0.82
Structure
x-ray diffraction · 3 distinct chains · 19% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E, G | IgG receptor fcrn large subunit P51 | protein | 263 | 27% helix, 41% strand | P55899 |
| B, D, F, H | Beta-2-microglobulin | protein | 99 | 0% helix, 49% strand | P61769 |
| I, J, K, L | Monomeric peptide inhibitor | protein | 13 | 0% helix, 46% strand | — |
Ligands and binding sites
- ACE · Acetyl group · ligand · 4 copies · chains I, J, K, L
- NH2 · Amino group · ion · 4 copies · chains I, J, G, K, L
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 806 | 0.82 | 0.85 | 93 | empty |
| 2 | 796 | 0.76 | 0.80 | 108 | empty |
| 3 | 562 | 0.68 | 0.78 | 72 | empty |
| 4 | 162 | 0.62 | 0.85 | 26 | empty |
| 5 | 358 | 0.61 | 0.77 | 48 | empty |
Interfaces
24 interfaces between chains.
- E–F · 1505 Ų buried · 27 hydrogen bonds · protein-protein
- C–D · 1502 Ų buried · 24 hydrogen bonds · protein-protein
- A–B · 1445 Ų buried · 21 hydrogen bonds · protein-protein
- G–H · 1428 Ų buried · 21 hydrogen bonds · protein-protein
- A–C · 964 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 disulfide, 12 modified, 4 covalent (disulfide, nonstandard, covalent ligand, methylation).
Compared structures
- 3M17 · Crystal structure of human FcRn with a monomeric peptide inhibitor · the same entry in another collection · chain L against L, 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 P55899
- Every structure of UniProt P61769
- Elsewhere: RCSB PDB 3M17 · PDBe 3M17 · UniProt P55899 · UniProt P61769
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.