MolNFT v1 · #56157 · protein
Crystal structure of human DAAM1 FH2
2Z6E · Disheveled-associated activator of morphogenesis 1: “Crystal structure of human DAAM1 FH2”. X-ray diffraction, 17 pockets (best druggability 0.64). MolNFT v1 #56157 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2Z6E
- Type
- protein
- Length
- 1,553 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Disheveled-associated activator of morphogenesis 1
- UniProt
- Q9Y4D1
- Pockets
- 17 · best druggability 0.64
Structure
x-ray diffraction · 4 distinct chains · 64% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Disheveled-associated activator of morphogenesis 1 | protein | 388 | 63% helix, 3% strand | Q9Y4D1 |
| B | Disheveled-associated activator of morphogenesis 1 | protein | 396 | 65% helix, 3% strand | Q9Y4D1 |
| C | Disheveled-associated activator of morphogenesis 1 | protein | 379 | 65% helix, 3% strand | Q9Y4D1 |
| D | Disheveled-associated activator of morphogenesis 1 | protein | 390 | 65% helix, 3% strand | Q9Y4D1 |
Pockets
17 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 350 | 0.64 | 0.80 | 23 | empty |
| 2 | 316 | 0.60 | 0.78 | 40 | empty |
| 3 | 230 | 0.50 | 0.75 | 31 | empty |
| 4 | 256 | 0.50 | 0.74 | 33 | empty |
| 5 | 130 | 0.49 | 0.80 | 22 | empty |
Interfaces
6 interfaces between chains.
- A–B · 5084 Ų buried · 70 hydrogen bonds · protein-protein
- C–D · 5083 Ų buried · 62 hydrogen bonds · protein-protein
- A–D · 288 Ų buried · 0 hydrogen bonds · protein-protein
- B–C · 221 Ų buried · 0 hydrogen bonds · protein-protein
- B–D · 62 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 Q9Y4D1
- Elsewhere: RCSB PDB 2Z6E · PDBe 2Z6E · UniProt Q9Y4D1
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