1R35: Nitric oxide synthase, inducible

Murine inducible nitric oxide synthase oxygenase dimer, tetrahydrobiopterin and 4R-fluoro-N6-ethanimidoyl-L-lysine. Determined by X-ray diffraction at 2.3 Å resolution. Released 5 Oct 2004.

Method: X-ray diffraction
Resolution: 2.3 Å
Organism: Mus musculus
Chains: 2
Atoms: 7,283
Mol. weight: 102.46 kDa
Ligands: I58, H4B, HEM
Released: 5 Oct 2004

Explore 1R35 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1R35 contains 54 α-helices and 46 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: 27 helices, 23 β-strands

Element	Residues	Length	Sheet
α-helix	78	1
β-strand	79-82	4	1
β-strand	89-92	4	1
α-helix	94-97	4
α-helix	117-119	3
β-strand	120	1	2
α-helix	127-129	3
α-helix	130-147	18
α-helix	153-170	18
α-helix	177-189	13
α-helix	197-199	3
β-strand	204-207	4	3
α-helix	214-229	16
α-helix	230-232	3
β-strand	237-240	4	3
α-helix	242-244	3
β-strand	252-253	2	4
β-strand	257	1	3
β-strand	261	1	5
β-strand	263-265	3	6
β-strand	271-273	3	6
α-helix	275-277	3
α-helix	278-286	9
α-helix	297	1
β-strand	298	1	5
α-helix	299-300	2
β-strand	301-304	4	4
α-helix	308-310	3
β-strand	311-313	3	4
β-strand	322-324	3	7
α-helix	333-336	4
β-strand	339-341	3	7
β-strand	345-346	2	3
β-strand	350-353	4	8
β-strand	356-358	3	8
β-strand	363-364	2	3
β-strand	367-368	2	9
α-helix	369-370	2
α-helix	371-376	6
α-helix	377-378	2
α-helix	386-393	8
α-helix	400-402	3
α-helix	404-422	19
β-strand	427-428	2	9
α-helix	432-448	17
α-helix	455-458	4
α-helix	464-466	3
α-helix	468-471	4
β-strand	482-484	3	8
β-strand	485	1	2

Chain B: 27 helices, 23 β-strands

Element	Residues	Length	Sheet
α-helix	78	1
β-strand	79-82	4	10
β-strand	89-92	4	10
α-helix	94-97	4
α-helix	117-119	3
β-strand	120	1	11
α-helix	127-129	3
α-helix	130-147	18
α-helix	153-170	18
α-helix	177-189	13
α-helix	197-199	3
β-strand	204-207	4	12
α-helix	214-229	16
α-helix	230-232	3
β-strand	237-240	4	12
α-helix	242-244	3
β-strand	252-253	2	13
β-strand	257	1	12
β-strand	261	1	14
β-strand	263-265	3	15
β-strand	271-273	3	15
α-helix	275-277	3
α-helix	278-286	9
α-helix	297	1
β-strand	298	1	14
α-helix	299-300	2
β-strand	301-304	4	13
α-helix	308-310	3
β-strand	311-313	3	13
β-strand	322-324	3	16
α-helix	333-336	4
β-strand	339-341	3	16
β-strand	345-346	2	12
β-strand	350-353	4	17
β-strand	356-358	3	17
β-strand	363-364	2	12
β-strand	367-368	2	18
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	18
α-helix	432-448	17
α-helix	455-458	4
α-helix	464-466	3
α-helix	468-471	4
β-strand	482-484	3	17
β-strand	485	1	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Nitric oxide synthase, inducible	A, B	protein	433	Mus musculus	P29477 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1R35_1 Nitric oxide synthase, inducible (chains A, B)
LDKLHVTSTRPQYVRIKNWGSGEILHDTLHHKATSDFTCKSKSCLGSIMNPKSLTRGPRD
KPTPLEELLPHAIEFINQYYGSFKEAKIEEHLARLEAVTKEIETTGTYQLTLDELIFATK
MAWRNAPRCIGRIQWSNLQVFDARNCSTAQEMFQHICRHILYATNNGNIRSAITVFPQRS
DGKHDFRLWNSQLIRYAGYQMPDGTIRGDAATLEFTQLCIDLGWKPRYGRFDVLPLVLQA
DGQDPEVFEIPPDLVLEVTMEHPKYEWFQELGLKWYALPAVANMLLEVGGLEFPACPFNG
WYMGTEIGVRDFCDTQRYNILEEVGRRMGLETHTLASLWKDRAVTEINVAVLHSFQKQNV
TIMDHHTASESFMKHMQNEYRARGGCPADWIWLVPPVSGSITPVFHQEMLNYVLSPFYYY
QIEPWKTHIWQNE

Ligands and cofactors

ID	Name	Formula	Copies
I58	4R-fluoro-N6-ethanimidoyl-L-lysine	C8 H16 F N3 O2	2
H4B	5,6,7,8-tetrahydrobiopterin	C9 H15 N5 O3	2
HEM	Protoporphyrin IX containing FE	C34 H32 Fe N4 O4	2

Water and common crystallization additives (SO4) are not listed.

Primary citation

4-Fluorinated L-lysine analogs as selective i-NOS inhibitors: methodology for introducing fluorine into the lysine side chain. Hallinan, E.A., Kramer, S.W., Houdek, S.C. et al. Org Biomol Chem (2003) 1:3527-3534. DOI 10.1039/b307563j · PubMed

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

3GOF 1.45 Å, Calmodulin bound to peptide from macrophage nitric oxide synthase
2ORT 1.87 Å, Murine Inducible Nitric Oxide Synthase Oxygenase Domain (Delta 114)…
2ORP 1.97 Å, Murine inducible nitric oxide synthase oxygenase domain (delta 114)…
2ORO 2.0 Å, Murine inducible nitric oxide synthase oxygenase domain (delta 114)…
2ORR 2.0 Å, Murine Inducible Nitric Oxide Synthase Oxygenase Domain (Delta 114)…
2ORS 2.0 Å, Murine Inducible Nitric Oxide Synthase Oxygenase Domain (DELTA 114)…
3E7M 2.0 Å, Structure of murine iNOS oxygenase domain with inhibitor AR-C95791
3E65 2.05 Å, Murine INOS dimer with HEME, pterin and inhibitor AR-C120011
1NOS 2.1 Å, Murine inducible nitric oxide synthase oxygenase domain (delta 114), imidazole complex
2ORQ 2.1 Å, Murine Inducible Nitric Oxide Synthase Oxygenase Domain (DELTA 114)…
3E68 2.2 Å, Structure of murine INOS oxygenase domain with inhibitor AR-C130232
3EAI 2.2 Å, Structure of inhibited murine iNOS oxygenase domain

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