Research workbench
Structure of the PHACTR1 rpel-2 bound to G-actin
Analyse Structure of the PHACTR1 rpel-2 bound to G-actin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4B1X
- Type
- protein
- Length
- 385 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Actin, alpha skeletal muscle; Phosphatase and actin regulator 1
- UniProt
- P68135, G5E8P7
- Ligands
- LAB, ATP, MG
- Pockets
- 2 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 46% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Actin, alpha skeletal muscle | protein | 357 | 45% helix, 20% strand | P68135 |
| M | Phosphatase and actin regulator 1 | protein | 28 | 57% helix, 0% strand | G5E8P7 |
Ligands and binding sites
- LAB · Latrunculin B · ligand · chains B
- ATP · Adenosine-5'-triphosphate · ligand · chains B
- MG · Magnesium ion · metal · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 361 | 0.72 | 0.84 | 47 | LAB, ATP, MG |
| 2 | 263 | 0.61 | 0.80 | 41 | empty |
Interfaces
1 interface between chains.
- B–M · 984 Ų buried · 13 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 P68135
- Every structure of UniProt G5E8P7
- Elsewhere: RCSB PDB 4B1X · PDBe 4B1X · UniProt P68135 · UniProt G5E8P7
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