Research workbench
Human DDAH-1, apo form
Analyse Human DDAH-1, apo form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7UT0
- Type
- protein
- Length
- 566 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.68
- Source
- Homo sapiens
- Molecule
- N(G),N(G)-dimethylarginine dimethylaminohydrolase 1
- EC
- 3.5.3.18
- UniProt
- O94760
- Pockets
- 7 · best druggability 0.83
Structure
x-ray diffraction · resolution 1.68 · 2 distinct chains · 33% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N(G),N(G)-dimethylarginine dimethylaminohydrolase 1 (EC 3.5.3.18) | protein | 284 | 32% helix, 24% strand | O94760 |
| B | N(G),N(G)-dimethylarginine dimethylaminohydrolase 1 (EC 3.5.3.18) | protein | 282 | 33% helix, 24% strand | O94760 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 376 | 0.83 | 0.91 | 35 | empty |
| 2 | 381 | 0.82 | 0.91 | 34 | empty |
| 3 | 365 | 0.66 | 0.80 | 54 | empty |
| 4 | 155 | 0.57 | 0.82 | 32 | empty |
| 5 | 169 | 0.46 | 0.76 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 555 Ų buried · 11 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 O94760
- Elsewhere: RCSB PDB 7UT0 · PDBe 7UT0 · UniProt O94760
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