Research workbench
Structure of human nnos R354A G357D mutant heme domain in complex with 7-((4-chloro-3-((METHYLAMINO)METHYL)PHENOXY) METHYL)QUINOLIN-2-amine
Analyse Structure of human nnos R354A G357D mutant heme domain in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5ADG
- Type
- protein
- Length
- 821 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nitric oxide synthase, brain
- UniProt
- P29475
- Ligands
- XEB, HEM, H4B, ZN
- Pockets
- 9 · best druggability 0.85
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nitric oxide synthase, brain | protein | 413 | 40% helix, 15% strand | P29475 |
| B | Nitric oxide synthase, brain | protein | 408 | 41% helix, 15% strand | P29475 |
Ligands and binding sites
- XEB · 7-[[4-chloranyl-3-(methylaminomethyl)phenoxy]methyl]quinolin-2-amine · ligand · 3 copies · chains A, B
- HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
- H4B · 5,6,7,8-tetrahydrobiopterin · ligand · 2 copies · chains A, B
- ZN · Zinc ion · metal · chains A, B
- GOL · Glycerol · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 586 | 0.85 | 0.90 | 94 | GOL, HEM, XEB |
| 2 | 330 | 0.79 | 0.89 | 53 | HEM, H4B, XEB |
| 3 | 80 | 0.64 | 0.91 | 14 | H4B |
| 4 | 121 | 0.43 | 0.76 | 26 | empty |
| 5 | 115 | 0.41 | 0.76 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 2808 Ų buried · 42 hydrogen bonds · protein-protein
Compared structures
- 5ADG · Structure of human nNOS R354A G357D mutant heme domain in complex with… · the same entry in another collection · chain A against A, 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 P29475
- Elsewhere: RCSB PDB 5ADG · PDBe 5ADG · UniProt P29475
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