Research workbench
Structure of human nnos heme domain with L-arg bound
Analyse Structure of human nnos heme domain with L-arg bound in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4D1N
- Type
- protein
- Length
- 1,662 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nitric oxide synthase, brain
- UniProt
- P29475
- Ligands
- ARG, HEM, H4B, ZN
- Pockets
- 19 · best druggability 0.86
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Nitric oxide synthase, brain | protein | 420 | 40% helix, 15% strand | P29475 |
| B, D | Nitric oxide synthase, brain | protein | 411 | 41% helix, 16% strand | P29475 |
Ligands and binding sites
- ARG · Arginine · ligand · 4 copies · chains A, B, C, D
- 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
- ZN · Zinc ion · metal · 2 copies · chains A, B, C, D
- GOL · Glycerol · additive · 7 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
19 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 846 | 0.86 | 0.88 | 89 | ARG, HEM, H4B |
| 2 | 1079 | 0.85 | 0.86 | 95 | ARG, HEM, H4B |
| 3 | 574 | 0.85 | 0.90 | 72 | ARG, HEM, H4B |
| 4 | 1189 | 0.84 | 0.85 | 92 | ARG, HEM, H4B |
| 5 | 259 | 0.76 | 0.89 | 34 | empty |
Interfaces
6 interfaces between chains.
- A–B · 2918 Ų buried · 43 hydrogen bonds · protein-protein
- C–D · 2863 Ų buried · 43 hydrogen bonds · protein-protein
- A–C · 913 Ų buried · 6 hydrogen bonds · protein-protein
- B–D · 625 Ų buried · 7 hydrogen bonds · protein-protein
- A–D · 214 Ų buried · 3 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 P29475
- Elsewhere: RCSB PDB 4D1N · PDBe 4D1N · UniProt P29475
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.