MolNFT v1 · #62159 · protein
Structure of human inosox with inhibitor ar-C95791
3E7G · Nitric oxide synthase, inducible: “Structure of human inosox with inhibitor ar-C95791”. X-ray diffraction, 4 ligands (HEM, H4B, AT2), 20 pockets (best druggability 0.86). MolNFT v1 #62159 on GenesisL1: 3D structure, binding sites…
- PDB
- 3E7G
- Type
- protein
- Length
- 1,686 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nitric oxide synthase, inducible
- EC
- 1.14.13.39
- UniProt
- P35228
- Ligands
- HEM, H4B, AT2, ZN
- Pockets
- 20 · best druggability 0.86
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, D | Nitric oxide synthase, inducible (EC 1.14.13.39) | protein | 421 | 41% helix, 15% strand | P35228 |
| C | Nitric oxide synthase, inducible (EC 1.14.13.39) | protein | 423 | 40% helix, 15% strand | P35228 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 4 copies · chains A, B, C, D
- H4B · 5,6,7,8-tetrahydrobiopterin · ligand · 4 copies · chains A, B, C, D
- AT2 · Ethyl 4-[(4-methylpyridin-2-yl)amino]piperidine-1-carboxylate · ligand · 4 copies · chains A, B, C, D
- ZN · Zinc ion · metal · 2 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 977 | 0.86 | 0.87 | 94 | HEM, H4B, AT2 |
| 2 | 1077 | 0.84 | 0.85 | 82 | HEM, H4B, AT2 |
| 3 | 1159 | 0.83 | 0.84 | 85 | HEM, H4B, AT2 |
| 4 | 1195 | 0.83 | 0.83 | 83 | HEM, H4B, AT2 |
| 5 | 63 | 0.70 | 0.97 | 22 | empty |
Interfaces
3 interfaces between chains.
- A–B · 2802 Ų buried · 34 hydrogen bonds · protein-protein
- C–D · 2746 Ų buried · 32 hydrogen bonds · protein-protein
- A–D · 361 Ų buried · 6 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 P35228
- Elsewhere: RCSB PDB 3E7G · PDBe 3E7G · UniProt P35228
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