Crystal Structure of Inducible Nitric Oxide Synthase with N-Nitrosated-pterin. Determined by X-ray diffraction at 2.2 Å resolution. Released 21 Jul 2010.
Explore 3NQS in 3D Show helices and sheets RCSB PDB PDBe
3NQS contains 58 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 | 79-82 | 4 | 1 |
| β-strand | 83 | 1 | 2 |
| β-strand | 89-92 | 4 | 1 |
| α-helix | 94-97 | 4 | |
| α-helix | 117-119 | 3 | |
| β-strand | 120 | 1 | 3 |
| α-helix | 127-129 | 3 | |
| α-helix | 130-145 | 16 | |
| α-helix | 153-170 | 18 | |
| α-helix | 177-189 | 13 | |
| α-helix | 197-199 | 3 | |
| β-strand | 204-207 | 4 | 4 |
| α-helix | 214-229 | 16 | |
| α-helix | 230-232 | 3 | |
| β-strand | 237-240 | 4 | 4 |
| α-helix | 241-244 | 4 | |
| β-strand | 252-253 | 2 | 5 |
| β-strand | 257 | 1 | 4 |
| β-strand | 261 | 1 | 6 |
| β-strand | 263-265 | 3 | 7 |
| β-strand | 271-273 | 3 | 7 |
| α-helix | 275-277 | 3 | |
| α-helix | 278-286 | 9 | |
| α-helix | 297 | 1 | |
| β-strand | 298 | 1 | 6 |
| α-helix | 299-300 | 2 | |
| β-strand | 301-304 | 4 | 5 |
| α-helix | 308-310 | 3 | |
| β-strand | 311-313 | 3 | 5 |
| α-helix | 314-316 | 3 | |
| α-helix | 317-319 | 3 | |
| β-strand | 322-324 | 3 | 8 |
| α-helix | 331-336 | 6 | |
| β-strand | 339-341 | 3 | 8 |
| β-strand | 345-346 | 2 | 4 |
| β-strand | 350-353 | 4 | 9 |
| β-strand | 356-358 | 3 | 9 |
| β-strand | 363-364 | 2 | 4 |
| β-strand | 367-368 | 2 | 10 |
| α-helix | 369-370 | 2 | |
| α-helix | 371-376 | 6 | |
| α-helix | 377-378 | 2 | |
| α-helix | 386-392 | 7 | |
| α-helix | 400-402 | 3 | |
| α-helix | 404-422 | 19 | |
| β-strand | 427-428 | 2 | 10 |
| α-helix | 430-448 | 19 | |
| α-helix | 455-458 | 4 | |
| α-helix | 464-466 | 3 | |
| α-helix | 468-471 | 4 | |
| β-strand | 472 | 1 | 2 |
| β-strand | 482-484 | 3 | 9 |
| β-strand | 485 | 1 | 3 |
| α-helix | 489-492 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 79-82 | 4 | 11 |
| β-strand | 83 | 1 | 12 |
| β-strand | 89-92 | 4 | 11 |
| α-helix | 94-97 | 4 | |
| α-helix | 117-119 | 3 | |
| β-strand | 120 | 1 | 13 |
| α-helix | 127-129 | 3 | |
| α-helix | 130-146 | 17 | |
| α-helix | 153-170 | 18 | |
| α-helix | 177-189 | 13 | |
| α-helix | 197-199 | 3 | |
| β-strand | 204-207 | 4 | 14 |
| α-helix | 214-229 | 16 | |
| α-helix | 230-232 | 3 | |
| β-strand | 237-240 | 4 | 14 |
| α-helix | 241-244 | 4 | |
| β-strand | 252-253 | 2 | 15 |
| β-strand | 257 | 1 | 14 |
| β-strand | 261 | 1 | 16 |
| β-strand | 263-265 | 3 | 17 |
| β-strand | 271-273 | 3 | 17 |
| α-helix | 275-277 | 3 | |
| α-helix | 278-286 | 9 | |
| α-helix | 297 | 1 | |
| β-strand | 298 | 1 | 16 |
| α-helix | 299-300 | 2 | |
| β-strand | 301-304 | 4 | 15 |
| α-helix | 308-310 | 3 | |
| β-strand | 311-313 | 3 | 15 |
| α-helix | 314-316 | 3 | |
| α-helix | 317-319 | 3 | |
| β-strand | 322-324 | 3 | 18 |
| α-helix | 331-336 | 6 | |
| β-strand | 339-341 | 3 | 18 |
| β-strand | 345-346 | 2 | 14 |
| β-strand | 350-353 | 4 | 19 |
| β-strand | 356-358 | 3 | 19 |
| β-strand | 363-364 | 2 | 14 |
| β-strand | 367-368 | 2 | 20 |
| α-helix | 369-370 | 2 | |
| α-helix | 371-376 | 6 | |
| α-helix | 377-378 | 2 | |
| α-helix | 386-392 | 7 | |
| α-helix | 400-402 | 3 | |
| α-helix | 404-422 | 19 | |
| β-strand | 427-428 | 2 | 20 |
| α-helix | 430-448 | 19 | |
| α-helix | 455-458 | 4 | |
| α-helix | 464-466 | 3 | |
| α-helix | 468-471 | 4 | |
| β-strand | 472 | 1 | 12 |
| β-strand | 482-484 | 3 | 19 |
| β-strand | 485 | 1 | 13 |
| α-helix | 489-492 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Nitric oxide synthase, inducible | A, B | protein | 433 | Mus musculus | P29477 (AlphaFold model) |
>3NQS_1 Nitric oxide synthase, inducible (chains A, B) LDKLHVTSTRPQYVRIKNWGSGEILHDTLHHKATSDFTCKSKSCLGSIMNPKSLTRGPRD KPTPLEELLPHAIEFINQYYGSFKEAKIEEHLARLEAVTKEIETTGTYQLTLDELIFATK MAWRNAPRCIGRIQWSNLQVFDARNCSTAQEMFQHICRHILYATNNGNIRSAITVFPQRS DGKHDFRLWNSQLIRYAGYQMPDGTIRGDAATLEFTQLCIDLGWKPRYGRFDVLPLVLQA DGQDPEVFEIPPDLVLEVTMEHPKYEWFQELGLKWYALPAVANMLLEVGGLEFPACPFNG WYMGTEIGVRDFCDTQRYNILEEVGRRMGLETHTLASLWKDRAVTEINVAVLHSFQKQNV TIMDHHTASESFMKHMQNEYRARGGCPADWIWLVPPVSGSITPVFHQEMLNYVLSPFYYY QIEPWKTHIWQNE
| 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 |
| NO | Nitric oxide | N O | 2 |
| AT2 | Ethyl 4-[(4-methylpyridin-2-yl)amino]piperidine-1-carboxylate | C14 H21 N3 O2 | 2 |
| BOG | octyl beta-D-glucopyranoside | C14 H28 O6 | 1 |
Water and common crystallization additives (GOL, EDO, SO4) are not listed.
Nitric-oxide synthase forms N-NO-pterin and S-NO-cys: implications for activity, allostery, and regulation. Rosenfeld, R.J., Bonaventura, J., Szymczyna, B.R. et al. J Biol Chem (2010) 285:31581-31589. DOI 10.1074/jbc.M109.072496 · PubMed
Other PDB entries of the same protein (UniProt P29477 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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