1DF1: Nitric oxide synthase

Murine inosoxy dimer with isothiourea bound in the active site. Determined by X-ray diffraction at 2.35 Å resolution. Released 8 Dec 1999.

Method
X-ray diffraction
Resolution
2.35 Å
Organism
Mus musculus
Chains
2
Atoms
7,198
Mol. weight
100.05 kDa
Ligands
ZN, HEM, H4B, ITU
Released
8 Dec 1999

Explore 1DF1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1DF1 contains 49 α-helices and 54 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.

Chain A: 24 helices, 27 β-strands

ElementResiduesLengthSheet
β-strand79-8241
β-strand8312
β-strand89-9241
α-helix94-974
β-strand10513
β-strand10813
α-helix117-1193
β-strand12014
α-helix130-14516
α-helix153-17018
α-helix177-18913
α-helix197-1993
β-strand204-20745
α-helix214-22916
α-helix230-2323
β-strand237-24045
α-helix242-2443
β-strand252-25326
β-strand25715
β-strand26117
β-strand263-26428
β-strand272-27328
α-helix275-2773
α-helix278-2869
β-strand29817
α-helix299-3002
β-strand301-30446
β-strand311-31336
β-strand322-32439
α-helix334-3363
β-strand339-34139
β-strand345-34625
β-strand350-353410
β-strand356-358310
β-strand363-36425
β-strand368111
α-helix369-3702
α-helix371-3766
α-helix377-3782
α-helix386-3916
α-helix400-4023
α-helix404-42219
β-strand428111
α-helix430-44819
α-helix455-4584
α-helix464-4663
α-helix468-4714
β-strand47212
β-strand482-484310
β-strand48514
α-helix489-4913
Chain B: 25 helices, 27 β-strands
ElementResiduesLengthSheet
β-strand79-82412
β-strand83113
β-strand89-92412
α-helix94-974
β-strand105114
β-strand108114
α-helix117-1193
β-strand120115
α-helix127-1293
α-helix130-14516
α-helix153-17018
α-helix177-18913
α-helix197-1993
β-strand204-207416
α-helix214-22916
α-helix230-2323
β-strand237-240416
α-helix241-2444
β-strand252-253217
β-strand257116
β-strand261118
β-strand263-265319
β-strand271-273319
α-helix275-2773
α-helix278-2869
β-strand298118
α-helix299-3002
β-strand301-304417
β-strand311-313317
α-helix317-3193
β-strand322-324320
α-helix334-3363
β-strand339-341320
β-strand345-346216
β-strand350-353421
β-strand356-358321
β-strand363-364216
β-strand368122
α-helix369-3702
α-helix371-3766
α-helix377-3782
α-helix386-3916
α-helix400-4023
α-helix404-42219
β-strand428122
α-helix430-44819
α-helix455-4584
α-helix468-4714
β-strand472113
β-strand482-484321
β-strand485115
α-helix489-4913

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Nitric oxide synthaseA, Bprotein423Mus musculusP29477 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>1DF1_1 NITRIC OXIDE SYNTHASE (chains A, B)
QYVRIKNWGSGEILHDTLHHKATSDFTCKSKSCLGSIMNPKSLTRGPRDKPTPLEELLPH
AIEFINQYYGSFKEAKIEEHLARLEAVTKEIETTGTYQLTLDELIFATKMAWRNAPRCIG
RIQWSNLQVFDARNCSTAQEMFQHICRHILYATNNGNIRSAITVFPQRSDGKHDFRLWNS
QLIRYAGYQMPDGTIRGDAATLEFTQLCIDLGWKPRYGRFDVLPLVLQADGQDPEVFEIP
PDLVLEVTMEHPKYEWFQELGLKWYALPAVANMLLEVGGLEFPACPFNGWYMGTEIGVRD
FCDTQRYNILEEVGRRMGLETHTLASLWKDRAVTEINVAVLHSFQKQNVTIMDHHTASES
FMKHMQNEYRARGGCPADWIWLVPPVSGSITPVFHQEMLNYVLSPFYYYQIEPWKTHIWQ
NEK

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn2
HEMProtoporphyrin IX containing FEC34 H32 Fe N4 O42
H4B5,6,7,8-tetrahydrobiopterinC9 H15 N5 O32
ITUEthylisothioureaC3 H8 N2 S2

Primary citation

N-terminal domain swapping and metal ion binding in nitric oxide synthase dimerization. Crane, B.R., Rosenfeld, R.J., Arvai, A.S. et al. EMBO J (1999) 18:6271-6281. DOI 10.1093/emboj/18.22.6271 · PubMed

Other PDB entries of the same protein (UniProt P29477 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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