3GOF: Calmodulin

Calmodulin bound to peptide from macrophage nitric oxide synthase. Determined by X-ray diffraction at 1.45 Å resolution. Released 31 Mar 2010.

Method: X-ray diffraction
Resolution: 1.45 Å
Organism: Gallus gallus
Chains: 4
Atoms: 3,181
Mol. weight: 38.21 kDa
Ligands: CA
Released: 31 Mar 2010

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

Secondary structure: helices and β-sheets

3GOF contains 20 α-helices and 8 β-strands across 4 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: 9 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	6-19	14
β-strand	26-27	2	1
α-helix	29-38	10
α-helix	45-55	11
β-strand	63-64	2	1
α-helix	65-77	13
α-helix	79-81	3
α-helix	82-92	11
β-strand	99-100	2	2
α-helix	102-112	11
α-helix	118-126	9
β-strand	136-137	2	2
α-helix	138-145	8

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	65-77	13
α-helix	82-92	11
β-strand	99-100	2	4
α-helix	102-112	11
α-helix	118-126	9
β-strand	136-137	2	4
α-helix	138-145	8

Chain C: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	4-6	3
α-helix	7-14	8

Chain D: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	7-14	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Calmodulin	A, B	protein	148	Gallus gallus	P62149 (AlphaFold model)
Nitric oxide synthase, inducible	C, D	protein	16		P29477 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>3GOF_1 Calmodulin (chains A, B)
ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGN
GTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEE
VDEMIREADIDGDGQVNYEEFVQMMTAK

Sequence of entity 2 (C, D), FASTA

>3GOF_2 Nitric oxide synthase, inducible (chains C, D)
RRREIRFRVLVKVVFF

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	8

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

Primary citation

Structural diversity in calmodulin recognition of nitric oxide synthases. Ng, H.L., Greenstein, A., Marletta, M. et al. To be published.

Other PDB entries of the same protein (UniProt P62149 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2O5G 1.08 Å, Calmodulin-smooth muscle light chain kinase peptide complex
3GP2 1.46 Å, Calmodulin bound to peptide from calmodulin kinase II (CaMKII)
2O60 1.55 Å, Calmodulin bound to peptide from neuronal nitric oxide synthase
1AHR 1.8 Å, Calmodulin mutant with a two residue deletion in the central helix
1UP5 1.9 Å, Chicken Calmodulin
2BCX 2.0 Å, Crystal structure of calmodulin in complex with a ryanodine receptor peptide
2VB6 2.3 Å, Myosin VI (MD-insert2-CaM, Delta Insert1) Post-rigor state (crystal form 2)
5HIT 2.85 Å, Crystal Structure Analysis of Ca2+-calmodulin and a C-terminal EAG1 channel fragment
2BKI 2.9 Å, Myosin VI nucleotide-free (MDinsert2-IQ) crystal structure
6BNV 4.6 Å, CryoEM structure of MyosinVI-actin complex in the rigor (nucleotide-free) state,…
2KZ2 Calmodulin, C-terminal domain, F92E mutant
2M3S Calmodulin, i85l, f92e, h107i, l112r, a128t, m144r mutant

Browse structure collections

About this viewer

MolViewer shows 3GOF directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.