Research workbench
The crystal structure of ternary PP1G-PPP1R15B and G-actin complex
Analyse The crystal structure of ternary PP1G-PPP1R15B and G-actin complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4V0U
- Type
- protein
- Length
- 3,390 residues
- Chains
- 15
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Actin, alpha skeletal muscle; SERINE/THREONINE-protein phosphatase PP1-gamma catalytic…
- EC
- 3.1.3.16
- UniProt
- P68135, P63087, Q5SWA1
- Ligands
- LAB, ATP, MN
- Pockets
- 20 · best druggability 0.83
Structure
x-ray diffraction · 3 distinct chains · 39% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, L, M | Actin, alpha skeletal muscle | protein | 364 | 45% helix, 21% strand | P68135 |
| D, F, H, J, N | SERINE/THREONINE-protein phosphatase PP1-gamma catalytic subunit (EC 3.1.3.16) | protein | 294 | 34% helix, 20% strand | P63087 |
| E, G, I, K, O | Protein phosphatase 1 regulatory subunit 15B | protein | 20 | 0% helix, 40% strand | Q5SWA1 |
Ligands and binding sites
- LAB · Latrunculin B · ligand · 5 copies · chains A, B, C, L, M
- ATP · Adenosine-5'-triphosphate · ligand · 5 copies · chains A, B, C, L, M
- MN · Manganese (II) ion · metal · 10 copies · chains D, F, H, J, N
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 930 | 0.83 | 0.85 | 115 | LAB, ATP |
| 2 | 996 | 0.79 | 0.81 | 83 | empty |
| 3 | 759 | 0.79 | 0.82 | 58 | empty |
| 4 | 587 | 0.77 | 0.83 | 40 | empty |
| 5 | 1083 | 0.76 | 0.79 | 80 | empty |
Interfaces
27 interfaces between chains.
- D–E · 1264 Ų buried · 32 hydrogen bonds · protein-protein
- H–I · 1256 Ų buried · 31 hydrogen bonds · protein-protein
- J–K · 1255 Ų buried · 33 hydrogen bonds · protein-protein
- F–G · 1253 Ų buried · 32 hydrogen bonds · protein-protein
- N–O · 1249 Ų buried · 32 hydrogen bonds · protein-protein
Compared structures
- 4V0U · The crystal structure of ternary PP1G-PPP1R15B and G-actin complex · the same entry in another collection · chain O against O, 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 P68135
- Every structure of UniProt P63087
- Every structure of UniProt Q5SWA1
- Elsewhere: RCSB PDB 4V0U · PDBe 4V0U · UniProt P68135 · UniProt P63087 · UniProt Q5SWA1
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