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Crystal structures of human pyy and npy
Analyse Crystal structures of human pyy and npy in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7RT9
- Type
- protein
- Length
- 907 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 4A3B2-a Fab heavy chain; 4A3B2-a Fab light chain; Peptide yy
- UniProt
- P10082
- Ligands
- NH2
- Pockets
- 6 · best druggability 0.67
Structure
x-ray diffraction · 6 distinct chains · 11% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 4A3B2-a Fab heavy chain | protein | 204 | 6% helix, 52% strand | — |
| B | 4A3B2-a Fab light chain | protein | 212 | 7% helix, 50% strand | — |
| C | 4A3B2-a Fab heavy chain | protein | 207 | 9% helix, 53% strand | — |
| D | 4A3B2-a Fab light chain | protein | 213 | 6% helix, 50% strand | — |
| Y | Peptide yy | protein | 36 | 56% helix, 0% strand | P10082 |
| Z | Peptide yy | protein | 35 | 57% helix, 0% strand | P10082 |
Ligands and binding sites
- NH2 · Amino group · ion · 2 copies · chains A, Y, C, Z
- GOL · Glycerol · additive · 2 copies · chains A, Y
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 809 | 0.67 | 0.74 | 84 | empty |
| 2 | 542 | 0.62 | 0.75 | 66 | empty |
| 3 | 54 | 0.55 | 0.90 | 22 | empty |
| 4 | 55 | 0.47 | 0.86 | 22 | empty |
| 5 | 100 | 0.42 | 0.78 | 17 | empty |
Interfaces
8 interfaces between chains.
- C–D · 1543 Ų buried · 9 hydrogen bonds · protein-protein
- A–B · 1500 Ų buried · 9 hydrogen bonds · protein-protein
- A–Y · 379 Ų buried · 4 hydrogen bonds · protein-protein
- C–Z · 350 Ų buried · 3 hydrogen bonds · protein-protein
- B–Y · 329 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 disulfide (disulfide).
Compared structures
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 P10082
- Elsewhere: RCSB PDB 7RT9 · PDBe 7RT9 · UniProt P10082
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