Dimethyladenosine transferase 2, mitochondrial

Intermolecular

Cysteine 591 of DNA-directed RNA polymerase, mitochondrial and cysteine 383 L

Intramolecular

A redox-regulated disulphide may form between cysteine 591 of DNA-directed RNA polymerase, mitochondrial and cysteine 383 of Dimethyladenosine transferase 2, mitochondrial. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

6erq

Structure name

structure of the human mitochondrial transcription initiation complex at the hsp promoter

Structure deposition date

2017-10-18

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide A name

DNA-directed RNA polymerase, mitochondrial

Peptide B name

Dimethyladenosine transferase 2, mitochondrial

Peptide A accession

O00411

Peptide B accession

Q9H5Q4

Peptide A residue number

591

Peptide B residue number

383

Ligandability

Cysteine 591 of DNA-directed RNA polymerase, mitochondrial

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 383 of Dimethyladenosine transferase 2, mitochondrial

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 Dimethyladenosine transferase 2, mitochondrial between cysteines 102 and 149. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?