MolNFT v1 · #188983 · protein
Human ddah-1, holo (zn-bound) form
7USZ · N(G),N(G)-dimethylarginine dimethylaminohydrolase 1: “Human ddah-1, holo (zn-bound) form”. X-ray diffraction, 2 ligands (ZN, CL), 5 pockets (best druggability 0.82). MolNFT v1 #188983 on GenesisL1: 3D structure, binding sites and…
- PDB
- 7USZ
- Type
- protein
- Length
- 560 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N(G),N(G)-dimethylarginine dimethylaminohydrolase 1
- EC
- 3.5.3.18
- UniProt
- O94760
- Ligands
- ZN, CL
- Pockets
- 5 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 32% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N(G),N(G)-dimethylarginine dimethylaminohydrolase 1 (EC 3.5.3.18) | protein | 274 | 32% helix, 26% strand | O94760 |
| B | N(G),N(G)-dimethylarginine dimethylaminohydrolase 1 (EC 3.5.3.18) | protein | 286 | 31% helix, 25% strand | O94760 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 375 | 0.82 | 0.91 | 31 | empty |
| 2 | 407 | 0.82 | 0.90 | 35 | empty |
| 3 | 200 | 0.66 | 0.85 | 32 | ZN |
| 4 | 134 | 0.62 | 0.86 | 28 | ZN |
| 5 | 154 | 0.39 | 0.73 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 99 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 O94760
- Elsewhere: RCSB PDB 7USZ · PDBe 7USZ · UniProt O94760
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