Research workbench
Crystal structure of endothelial nitric oxide synthase peptide bound to calmodulin
Analyse Crystal structure of endothelial nitric oxide synthase peptide bound to… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1NIW
- Type
- protein
- Length
- 656 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Calmodulin; Nitric-oxide synthase, endothelial
- EC
- 1.14.13.39
- UniProt
- P62161, P29474
- Ligands
- CA, SO4
- Pockets
- 5 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 62% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E, G | Calmodulin | protein | 145 | 60% helix, 4% strand | P62161 |
| B, D, F, H | Nitric-oxide synthase, endothelial (EC 1.14.13.39) | protein | 19 | 74% helix, 0% strand | P29474 |
Ligands and binding sites
- CA · Calcium ion · metal · 16 copies · chains A, C, E, G
- SO4 · Sulfate ion · ion · chains A, E
- EDO · 1,2-ethanediol · additive · 4 copies · chains A, C, E, G
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1093 | 0.74 | 0.77 | 110 | SO4, EDO |
| 2 | 346 | 0.56 | 0.75 | 48 | empty |
| 3 | 118 | 0.46 | 0.79 | 25 | empty |
| 4 | 66 | 0.35 | 0.77 | 12 | empty |
| 5 | 57 | 0.30 | 0.75 | 13 | empty |
Interfaces
9 interfaces between chains.
- E–F · 1379 Ų buried · 5 hydrogen bonds · protein-protein
- C–D · 1355 Ų buried · 8 hydrogen bonds · protein-protein
- A–B · 1341 Ų buried · 4 hydrogen bonds · protein-protein
- G–H · 1338 Ų buried · 9 hydrogen bonds · protein-protein
- A–E · 328 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 36 modified (engineered).
Compared structures
- 1NIW · Crystal structure of endothelial nitric oxide synthase peptide bound to calmodulin · 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 P62161
- Every structure of UniProt P29474
- Elsewhere: RCSB PDB 1NIW · PDBe 1NIW · UniProt P62161 · UniProt P29474
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