8FMO: Troponin C, slow skeletal and cardiac muscles

Complex structure of K210 deletion Troponin complex with risedronate. Determined by X-ray diffraction at 2.61 Å resolution. Released 31 Jan 2024.

Method: X-ray diffraction
Resolution: 2.61 Å
Organism: Homo sapiens
Chains: 6
Atoms: 5,425
Mol. weight: 94.34 kDa
Ligands: CA
Released: 31 Jan 2024

Explore 8FMO in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8FMO contains 30 α-helices and 8 β-strands across 6 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	2-10	9
α-helix	14-27	14
β-strand	36	1	1
α-helix	38-47	10
α-helix	56-64	9
β-strand	72	1	1
α-helix	74-82	9
α-helix	94-104	11
β-strand	112-113	2	2
α-helix	114-123	10
α-helix	130-140	11
β-strand	147-148	2	2
α-helix	150-156	7

Chains B and E: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	207-220	14
α-helix	225-269	45

Chains C and F: 4 helices, 0 β-strands

Element	Residues	Length
α-helix	43-79	37
α-helix	81-83	3
α-helix	90-134	45
α-helix	152-158	7

Chain D: 9 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	2-10	9
α-helix	14-27	14
β-strand	36	1	3
α-helix	38-46	9
α-helix	54-63	10
β-strand	72	1	3
α-helix	74-83	10
α-helix	94-104	11
β-strand	112-113	2	4
α-helix	114-123	10
α-helix	130-140	11
β-strand	147-148	2	4
α-helix	150-156	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Troponin C, slow skeletal and cardiac muscles	A, D	protein	164	Homo sapiens	P63316 (AlphaFold model)
Troponin T, cardiac muscle	B, E	protein	108	Homo sapiens	P45379 (AlphaFold model)
Troponin I, cardiac muscle	C, F	protein	135	Homo sapiens	P19429 (AlphaFold model)

Sequence of entity 1 (A, D), FASTA

>8FMO_1 Troponin C, slow skeletal and cardiac muscles (chains A, D)
QGSMDDIYKAAVEQLTEEQKNEFKAAFDIFVLGAEDGSISTKELGKVMRMLGQNPTPEEL
QEMIDEVDEDGSGTVDFDEFLVMMVRSMKDDSKGKSEEELSDLFRMFDKNADGYIDLEEL
KIMLQATGETITEDDIEELMKDGDKNNDGRIDYDEFLEFMKGVE

Sequence of entity 2 (B, E), FASTA

>8FMO_2 Troponin T, cardiac muscle (chains B, E)
QGSHFGGYIQKQAQTERKSGKRQTEREKKKILAERRKVLAIDHLNEDQLREKAKELWQSI
YNLEAEKFDLQEKFKQQKYEINVLRNRINDNQKVSKTRGKAKVTGRWK

Sequence of entity 3 (C, F), FASTA

>8FMO_3 Troponin I, cardiac muscle (chains C, F)
EPHAKKKSKISASRKLQLKTLLLQIAKQELEREAEERRGEKGRALSTRAQPLELAGLGFA
ELQDLARQLHARVDKVDEERYDIEAKVTKNITEIADLTQKIFDLRGKFKRPTLRRVRISA
DAMMQALLGARAKES

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	6

Primary citation

Structural and Phenotypic Correction of K210del Genetic Cardiomyopathy by an FDA Approved drug. Wang, P., Ahmed, M., Sadek, H. To be published.

Other PDB entries of the same protein (UniProt P63316 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3SD6 1.37 Å, Crystal structure of the amino-terminal domain of human cardiac troponin C in complex…
4GJE 1.6 Å, Crystal structure of the refolded amino-terminal domain of human cardiac troponin C in…
3SWB 1.67 Å, Crystal structure of the amino-terminal domain of human cardiac troponin C in complex…
7SC2 1.81 Å, Crystal structure of the N-domain of cardiac muscle troponin C tethered to the switch…
4GJF 1.9 Å, Crystal structure of the amino-terminal domain of human cardiac troponin C mutant L29Q…
4GJG 2.0 Å, Crystal structure of the amino-terminal domain of human cardiac troponin C mutant…
4Y99 2.0 Å, Core domain of human cardiac troponin
1WRK 2.15 Å, Crystal structure of the N-terminal domain of human cardiac troponin C in complex with…
3RV5 2.2 Å, Crystal structure of human cardiac troponin C regulatory domain in complex with cadmium…
7SC3 2.23 Å, Crystal structure of the N-domain of cardiac muscle troponin C tethered to the switch…
1WRL 2.6 Å, Crystal structure of the N-terminal domain of human cardiac troponin C in complex with…
1J1D 2.61 Å, Crystal structure of the 46kDa domain of human cardiac troponin in the Ca2+ saturated form

Browse structure collections

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