Structure of rat neuronal nitric oxide synthase heme domain in complex with 6-(2,3-difluoro-5-(3-(methylamino)prop-1-yn-1-yl)phenethyl)-4-methylpyridin-2-amine. Determined by X-ray diffraction at 1.77 Å resolution. Released 13 Mar 2019.
Explore 6NGX in 3D Show helices and sheets RCSB PDB PDBe
6NGX contains 54 α-helices and 50 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 301-304 | 4 | 1 |
| β-strand | 305 | 1 | 2 |
| β-strand | 311-314 | 4 | 1 |
| α-helix | 316-319 | 4 | |
| β-strand | 331 | 1 | 3 |
| α-helix | 348-350 | 3 | |
| α-helix | 351-368 | 18 | |
| α-helix | 375-391 | 17 | |
| α-helix | 398-410 | 13 | |
| α-helix | 418-420 | 3 | |
| β-strand | 425-428 | 4 | 4 |
| α-helix | 435-450 | 16 | |
| α-helix | 451-453 | 3 | |
| β-strand | 458-461 | 4 | 4 |
| α-helix | 462-465 | 4 | |
| β-strand | 473-474 | 2 | 5 |
| β-strand | 478 | 1 | 4 |
| β-strand | 482 | 1 | 6 |
| β-strand | 484-486 | 3 | 7 |
| β-strand | 492-494 | 3 | 7 |
| α-helix | 496-498 | 3 | |
| α-helix | 499-506 | 8 | |
| α-helix | 518 | 1 | |
| β-strand | 519 | 1 | 6 |
| α-helix | 520-521 | 2 | |
| β-strand | 522-525 | 4 | 5 |
| β-strand | 532-534 | 3 | 5 |
| α-helix | 535-537 | 3 | |
| α-helix | 538-540 | 3 | |
| β-strand | 543-545 | 3 | 8 |
| α-helix | 552-557 | 6 | |
| β-strand | 560-562 | 3 | 8 |
| β-strand | 566-567 | 2 | 4 |
| β-strand | 571-574 | 4 | 9 |
| β-strand | 577-579 | 3 | 9 |
| β-strand | 584-585 | 2 | 4 |
| β-strand | 588-589 | 2 | 10 |
| α-helix | 590-591 | 2 | |
| α-helix | 592-597 | 6 | |
| α-helix | 598-599 | 2 | |
| α-helix | 607-614 | 8 | |
| α-helix | 621-623 | 3 | |
| α-helix | 625-643 | 19 | |
| β-strand | 648-649 | 2 | 10 |
| α-helix | 651-669 | 19 | |
| α-helix | 676-679 | 4 | |
| α-helix | 685-687 | 3 | |
| α-helix | 689-692 | 4 | |
| β-strand | 693 | 1 | 2 |
| β-strand | 697 | 1 | 11 |
| β-strand | 703-705 | 3 | 9 |
| α-helix | 710-712 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 301-304 | 4 | 12 |
| β-strand | 305 | 1 | 13 |
| β-strand | 311-314 | 4 | 12 |
| α-helix | 316-319 | 4 | |
| β-strand | 331 | 1 | 11 |
| α-helix | 351-368 | 18 | |
| α-helix | 375-391 | 17 | |
| α-helix | 398-410 | 13 | |
| α-helix | 418-420 | 3 | |
| β-strand | 425-428 | 4 | 14 |
| α-helix | 435-450 | 16 | |
| α-helix | 451-453 | 3 | |
| β-strand | 458-461 | 4 | 14 |
| α-helix | 462-465 | 4 | |
| β-strand | 473-474 | 2 | 15 |
| β-strand | 478 | 1 | 14 |
| β-strand | 482 | 1 | 16 |
| β-strand | 484-486 | 3 | 17 |
| β-strand | 492-494 | 3 | 17 |
| α-helix | 496-498 | 3 | |
| α-helix | 499-507 | 9 | |
| α-helix | 518 | 1 | |
| β-strand | 519 | 1 | 16 |
| α-helix | 520-521 | 2 | |
| β-strand | 522-525 | 4 | 15 |
| α-helix | 529-531 | 3 | |
| β-strand | 532-534 | 3 | 15 |
| α-helix | 535-537 | 3 | |
| α-helix | 538-540 | 3 | |
| β-strand | 543-545 | 3 | 18 |
| α-helix | 552-557 | 6 | |
| β-strand | 560-562 | 3 | 18 |
| β-strand | 566-567 | 2 | 14 |
| β-strand | 571-574 | 4 | 19 |
| β-strand | 577-579 | 3 | 19 |
| β-strand | 584-585 | 2 | 14 |
| β-strand | 588-589 | 2 | 20 |
| α-helix | 590-591 | 2 | |
| α-helix | 592-597 | 6 | |
| α-helix | 598-599 | 2 | |
| α-helix | 607-614 | 8 | |
| α-helix | 621-623 | 3 | |
| α-helix | 625-643 | 19 | |
| β-strand | 648-649 | 2 | 20 |
| α-helix | 651-669 | 19 | |
| α-helix | 676-679 | 4 | |
| α-helix | 685-687 | 3 | |
| α-helix | 689-692 | 4 | |
| β-strand | 693 | 1 | 13 |
| β-strand | 697 | 1 | 3 |
| β-strand | 703-705 | 3 | 19 |
| α-helix | 710-713 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Nitric oxide synthase, brain | A, B | protein | 422 | Rattus norvegicus | P29476 (AlphaFold model) |
>6NGX_1 Nitric oxide synthase, brain (chains A, B) CPRFLKVKNWETDVVLTDTLHLKSTLETGCTEHICMGSIMLPSQHTRKPEDVRTKDQLFP LAKEFLDQYYSSIKRFGSKAHMDRLEEVNKEIESTSTYQLKDTELIYGAKHAWRNASRCV GRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLRSAITIFPQRTDGKHDFRVWN SQLIRYAGYKQPDGSTLGDPANVQFTEICIQQGWKAPRGRFDVLPLLLQANGNDPELFQI PPELVLEVPIRHPKFDWFKDLGLKWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGVR DYCDNSRYNILEEVAKKMDLDMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATE SFIKHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEMLNYRLTPSFEYQPDPWNTHVW KG
| ID | Name | Formula | Copies |
|---|---|---|---|
| HEM | Protoporphyrin IX containing FE | C34 H32 Fe N4 O4 | 2 |
| H4B | 5,6,7,8-tetrahydrobiopterin | C9 H15 N5 O3 | 2 |
| KMV | 6-(2-{2,3-difluoro-5-[3-(methylamino)prop-1-yn-1-yl]phenyl}ethyl)-4-methylpyrid… | C18 H19 F2 N3 | 2 |
| ZN | Zinc ion | Zn | 1 |
Water and common crystallization additives (ACT, GOL) are not listed.
Optimization of Blood-Brain Barrier Permeability with Potent and Selective Human Neuronal Nitric Oxide Synthase Inhibitors Having a 2-Aminopyridine Scaffold. Do, H.T., Li, H., Chreifi, G. et al. J Med Chem (2019) 62:2690-2707. DOI 10.1021/acs.jmedchem.8b02032 · PubMed
Other PDB entries of the same protein (UniProt P29476 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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