Research workbench
Hexamer formed by a macrocyclic peptide derived from beta-2- microglobulin (63-69) - (ORN)YLL(PHI)YTE(ORN)KVT(MAA)TVK
Analyse Hexamer formed by a macrocyclic peptide derived from beta-2- microglobulin… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4P4Y
- Type
- protein
- Length
- 112 residues
- Chains
- 7
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cyclic hexadecapeptide (ORN)YLL(PHI)YTE(ORN)KVT(MAA)TVK
- Ligands
- CL, SO4
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 56% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G | Cyclic hexadecapeptide (ORN)YLL(PHI)YTE(ORN)KVT(MAA)TVK | protein | 16 | 0% helix, 56% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
7 interfaces between chains.
- A–B · 384 Ų buried · 9 hydrogen bonds · protein-protein
- D–E · 238 Ų buried · 0 hydrogen bonds · protein-protein
- A–C · 236 Ų buried · 0 hydrogen bonds · protein-protein
- E–F · 215 Ų buried · 0 hydrogen bonds · protein-protein
- B–C · 206 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 28 modified (nonstandard).
Compared structures
- 4P4Y · Hexamer formed by a macrocyclic peptide derived from beta-2-microglobulin (63-69)… · the same entry in another collection · chain F against F, 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
- Elsewhere: RCSB PDB 4P4Y · PDBe 4P4Y
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.