N6-adenosine-methyltransferase catalytic subunit
Intermolecular
Cysteine 500 and cysteine 120 of N6-adenosine-methyltransferase non-catalytic subunit L
Intramolecular
Cysteine 375 and cysteine 376
7o0q A 500 B 120
A redox-regulated disulphide may form between cysteine 500 of N6-adenosine-methyltransferase catalytic subunit and cysteine 120 of N6-adenosine-methyltransferase non-catalytic subunit. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
7o0q
Structure name
crystal structure of the human mettl3-mettl14 complex bound to compound 12 (ado_ad_066)
Structure deposition date
2021-03-26
Thiol separation (Å)
7
Half-sphere exposure sum ?
81
Minimum pKa ?
11
% buried
83
Peptide A name
N6-adenosine-methyltransferase catalytic subunit
Peptide B name
N6-adenosine-methyltransferase non-catalytic subunit
Peptide A accession
Q86U44
Peptide B accession
Q9HCE5
Peptide A residue number
500
Peptide B residue number
120
Ligandability
Cysteine 500 of N6-adenosine-methyltransferase catalytic subunit
Cysteine 120 of N6-adenosine-methyltransferase non-catalytic subunit
7o27 A 375 A 376
A redox-regulated disulphide may form within N6-adenosine-methyltransferase catalytic subunit between cysteines 375 and 376. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
52
PDB code
7o27
Structure name
crystal structure of the human mettl3-mettl14 complex bound to compound 17 (ado_ae_005)
Structure deposition date
2021-03-30
Thiol separation (Å)
7
Half-sphere exposure sum ?
59
Minimum pKa ?
10
% buried
48
Peptide accession
Q86U44
Residue number A
375
Residue number B
376
Peptide name
N6-adenosine-methyltransferase catalytic subunit
Ligandability
Cysteine 375 of N6-adenosine-methyltransferase catalytic subunit
Cysteine 376 of N6-adenosine-methyltransferase catalytic subunit
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