3HR4: Human iNOS Reductase and Calmodulin Complex

Human iNOS Reductase and Calmodulin Complex. Determined by X-ray diffraction at 2.5 Å resolution. Released 8 Sept 2009.

Method: X-ray diffraction
Resolution: 2.5 Å
Organism: Homo sapiens
Chains: 8
Atoms: 10,594
Mol. weight: 170.06 kDa
Ligands: CA, FMN
Released: 8 Sept 2009

Explore 3HR4 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3HR4 contains 68 α-helices and 48 β-strands across 8 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: 10 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	515-534	20
β-strand	538-544	7	1
α-helix	549-561	13
β-strand	566-571	6	1
α-helix	572-574	3
α-helix	577-581	5
β-strand	585-591	7	1
β-strand	593	1	2
β-strand	597	1	2
α-helix	600-602	3
α-helix	603-611	9
β-strand	620-627	8	1
α-helix	636-648	13
β-strand	651-652	2	1
α-helix	655-656	2
β-strand	657-660	4	1
α-helix	665-683	19
α-helix	689-691	3

Chain B: 8 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	6-19	14
β-strand	26-27	2	3
α-helix	29-38	10
α-helix	45-55	11
β-strand	63-64	2	3
α-helix	65-76	12
α-helix	81-92	12
β-strand	100	1	4
α-helix	102-111	10
α-helix	118-126	9
β-strand	136	1	4
α-helix	138-145	8

Chain C: 9 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	515-535	21
α-helix	537	1
β-strand	538-544	7	5
α-helix	552-561	10
β-strand	566-571	6	5
α-helix	577-581	5
β-strand	585-591	7	5
β-strand	593	1	6
β-strand	597	1	6
α-helix	598-599	2
α-helix	600-611	12
β-strand	620-627	8	5
α-helix	636-647	12
β-strand	651-660	10	5
α-helix	665-682	18
α-helix	689-691	3

Chain D: 8 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	6-19	14
β-strand	26-27	2	7
α-helix	29-38	10
α-helix	45-55	11
β-strand	63-64	2	7
α-helix	65-75	11
α-helix	81-92	12
β-strand	99-100	2	8
α-helix	102-111	10
α-helix	118-125	8
β-strand	136-137	2	8
α-helix	138-146	9

Chain E: 9 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	515-533	19
β-strand	540-543	4	9
α-helix	549-560	12
α-helix	561-563	3
β-strand	568-571	4	9
α-helix	572-574	3
α-helix	577-580	4
β-strand	585-591	7	9
β-strand	593	1	10
β-strand	597	1	10
α-helix	600-602	3
α-helix	603-609	7
β-strand	620-627	8	9
α-helix	636-647	12
β-strand	651-660	10	9
β-strand	663-664	2	9
α-helix	665-677	13

Chain F: 8 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	6-19	14
β-strand	26-27	2	11
α-helix	29-38	10
α-helix	45-53	9
β-strand	63-64	2	11
α-helix	65-76	12
α-helix	82-92	11
β-strand	99-100	2	12
α-helix	102-111	10
α-helix	118-125	8
β-strand	136-137	2	12
α-helix	138-145	8

Chain G: 7 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	515-534	20
β-strand	537-538	2	13
β-strand	539-544	6	14
α-helix	549-561	13
β-strand	565-566	2	13
β-strand	571	1	14
α-helix	577-579	3
β-strand	585-591	7	14
β-strand	593	1	15
β-strand	597	1	15
α-helix	598-599	2
α-helix	604-610	7
β-strand	620-627	8	14
α-helix	636-648	13
β-strand	651-660	10	14
α-helix	661-682	22

Chain H: 9 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	6-19	14
β-strand	26	1	16
α-helix	29-36	8
α-helix	37-39	3
α-helix	45-55	11
β-strand	64	1	16
α-helix	65-75	11
α-helix	82-90	9
β-strand	100	1	17
α-helix	102-111	10
α-helix	118-126	9
β-strand	136	1	17
α-helix	139-145	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Nitric oxide synthase, inducible	A, C, E, G	protein	219	Homo sapiens	P35228 (AlphaFold model)
Calmodulin	B, D, F, H	protein	149	Homo sapiens	P0DP23 (AlphaFold model)

Sequence of entity 1 (A, C, E, G), FASTA

>3HR4_1 Nitric oxide synthase, inducible (chains A, C, E, G)
HHHHHHDEKRRPKRREIPLKVLVKAVLFACMLMRKTMASRVRVTILFATETGKSEALAWD
LGALFSCAFNPKVVCMDKYRLSCLEEERLLLVVTSTFGNGDCPGNGEKLKKSLFMLKELN
NKFRYAVFGLGSSMYPRFCAFAHDIDQKLSHLGASQLTPMGEGDELSGQEDAFRSWAVQT
FKAACETFDVRGKQHIQIPKLYTSNVTWDPHHYRLVQDS

Sequence of entity 2 (B, D, F, H), FASTA

>3HR4_2 Calmodulin (chains B, D, F, H)
MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADG
NGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDE
EVDEMIREADIDGDGQVNYEEFVQMMTAK

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	16
FMN	Flavin mononucleotide	C17 H21 N4 O9 P	4

Primary citation

Regulation of Interdomain Interactions by CaM in Inducible Nitric Oxide Synthase. Xia, C., Misra, I., Iyanaki, T. et al. J Biol Chem (2009).

Other PDB entries of the same protein (UniProt P35228 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6JWM 1.23 Å, Crystal structure of the SPRY domain of SPSB2 in complex with cR7, a potent cyclic…
6KEY 1.24 Å, Structural basis for the regulation of inducible nitric oxide synthase (iNOS) by the…
5XN3 1.34 Å, Crystal structure of SPSB2 in complex with a rational designed RGD containing cyclic…
6JWN 1.61 Å, Crystal structure of the SPRY domain of SPSB2 in complex with cR9, a cyclic peptide…
3E7G 2.2 Å, Structure of human INOSOX with inhibitor AR-C95791
4NOS 2.25 Å, Human inducible nitric oxide synthase with inhibitor
1NSI 2.55 Å, Human inducible nitric oxide synthase, ZN-bound, L-arg complex
3EJ8 2.55 Å, Structure of double mutant of human iNOS oxygenase domain with bound immidazole
2NSI 3.0 Å, Human inducible nitric oxide synthase, ZN-free, seitu complex
4CX7 3.16 Å, Structure of human iNOS heme domain in complex with (R)-6-(3-AMINO-2-(5-(2-(6-AMINO-4-…
2LL6 Solution NMR structure of CaM bound to iNOS CaM binding domain peptide
5TP6 Solution structure of the CaM34 with the iNOS CaM binding domain peptide

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