MolNFT v1 · #108032 · protein
Human dynamin 1 K44A superconstricted polymer stabilized with GTP strand 2
4UUK · Dynamin-1: “Human dynamin 1 K44A superconstricted polymer stabilized with GTP strand 2”. Electron microscopy, 20 pockets (best druggability 0.74). MolNFT v1 #108032 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4UUK
- Type
- protein
- Length
- 2,616 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dynamin-1
- EC
- 3.6.5.5
- UniProt
- Q05193
- Pockets
- 20 · best druggability 0.74
Structure
electron microscopy · 4 distinct chains · 48% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, G | Dynamin-1 (EC 3.6.5.5) | protein | 329 | 47% helix, 12% strand | Q05193 |
| B, E, I, J | Dynamin-1 (EC 3.6.5.5) | protein | 208 | 74% helix, 0% strand | Q05193 |
| C, F, H, L | Dynamin-1 (EC 3.6.5.5) | protein | 113 | 14% helix, 37% strand | Q05193 |
| D, K | Dynamin-1 (EC 3.6.5.5) | protein | 337 | 45% helix, 10% strand | Q05193 |
Pockets
20 pockets found on a 1 Å grid, 17 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 266 | 0.74 | 0.87 | 36 | empty |
| 2 | 254 | 0.72 | 0.87 | 38 | empty |
| 3 | 79 | 0.70 | 0.94 | 21 | empty |
| 4 | 79 | 0.69 | 0.94 | 21 | empty |
| 5 | 324 | 0.65 | 0.81 | 35 | empty |
Interfaces
12 interfaces between chains.
- E–I · 1572 Ų buried · 31 hydrogen bonds · protein-protein
- B–J · 1565 Ų buried · 31 hydrogen bonds · protein-protein
- B–E · 1225 Ų buried · 40 hydrogen bonds · protein-protein
- D–E · 700 Ų buried · 16 hydrogen bonds · protein-protein
- J–K · 698 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
- 4UUK · Human dynamin 1 K44A superconstricted polymer stabilized with GTP strand 2 · the same entry in another collection · chain L against L, 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 Q05193
- Elsewhere: RCSB PDB 4UUK · PDBe 4UUK · UniProt Q05193
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