Myosin-binding protein C, cardiac-type

Intramolecular

A redox-regulated disulphide may form within Myosin-binding protein C, cardiac-type between cysteines 237 and 248 (460 and 471 respectively in this structure).

Details

Redox score ?

PDB code

4edq

Structure name

mbp-fusion protein of myosin-binding protein c residues 149-269

Structure deposition date

2012-03-27

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

O70468

Residue number A

237

Residue number B

248

Peptide name

Myosin-binding protein C, cardiac-type

Ligandability

Cysteine 237 of Myosin-binding protein C, cardiac-type

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 248 of Myosin-binding protein C, cardiac-type

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Myosin-binding protein C, cardiac-type between cysteines 436 and 443 (286 and 293 respectively in this structure).

Details

Redox score ?

PDB code

1pd6

Structure name

the nmr structure of domain c2 of human cardiac myosin binding protein c

Structure deposition date

2003-05-19

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Q14896

Residue number A

436

Residue number B

443

Peptide name

Myosin-binding protein C, cardiac-type

Ligandability

Cysteine 436 of Myosin-binding protein C, cardiac-type

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 443 of Myosin-binding protein C, cardiac-type

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Myosin-binding protein C, cardiac-type between cysteines 239 and 249. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?