MolNFT v1 · #182380 · protein
Crystal structure of native bovine arrestin 1 in complex with 1,5-di- methylenebisphosphonate inositol tetrakisphosphate (1,5-pcp-IP4)
7MP1 · S-arrestin: “Crystal structure of native bovine arrestin 1 in complex with 1,5-di- methylenebisphosphonate inositol…”. X-ray diffraction, 1 ligand (4WZ), 16 pockets (best druggability 0.73). MolNFT v1 #182380 on GenesisL1: 3D…
- PDB
- 7MP1
- Type
- protein
- Length
- 1,462 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- S-arrestin
- UniProt
- P08168
- Ligands
- 4WZ
- Pockets
- 16 · best druggability 0.73
Structure
x-ray diffraction · 4 distinct chains · 5% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | S-arrestin | protein | 370 | 5% helix, 49% strand | P08168 |
| B | S-arrestin | protein | 361 | 6% helix, 51% strand | P08168 |
| C | S-arrestin | protein | 363 | 6% helix, 49% strand | P08168 |
| D | S-arrestin | protein | 368 | 5% helix, 50% strand | P08168 |
Ligands and binding sites
- 4WZ · {[(1R,3S,4S,5R,6S)-2,4,5,6-tetrakis(phosphonooxy) cyclohexane-1,3-diyl]bis[oxy(hydroxyphosphoryl) methanediyl]}bis(phosphonic acid) · ligand · 5 copies · chains B, C, A, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
16 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1108 | 0.73 | 0.77 | 103 | empty |
| 2 | 1052 | 0.72 | 0.76 | 99 | empty |
| 3 | 170 | 0.54 | 0.80 | 28 | empty |
| 4 | 104 | 0.53 | 0.83 | 22 | empty |
| 5 | 100 | 0.52 | 0.83 | 21 | empty |
Interfaces
5 interfaces between chains.
- B–C · 1105 Ų buried · 15 hydrogen bonds · protein-protein
- A–D · 1088 Ų buried · 12 hydrogen bonds · protein-protein
- C–D · 609 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 585 Ų buried · 11 hydrogen bonds · protein-protein
- B–D · 13 Ų buried · 0 hydrogen bonds · protein-protein
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 P08168
- Elsewhere: RCSB PDB 7MP1 · PDBe 7MP1 · UniProt P08168
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