DNA primase large subunit
Intermolecular
Cysteine 449 and cysteine 449
Intramolecular
Cysteine 367 and cysteine 424
Cysteine 287 and cysteine 384
Cysteine 367 and cysteine 384
Cysteine 287 and cysteine 367
Cysteine 287 and cysteine 424
Cysteine 384 and cysteine 424
Cysteine 424 and cysteine 437
3l9q A 449 B 449
A redox-regulated disulphide may form between two units of DNA primase large subunit at cysteines 449 and 449.
Details
Redox score ?
79
PDB code
3l9q
Structure name
crystal structure of human polymerase alpha-primase p58 iron-sulfur cluster domain
Structure deposition date
2010-01-05
Thiol separation (Å)
2
Half-sphere exposure sum ?
83
Minimum pKa ?
nan
% buried
nan
Peptide A name
DNA primase large subunit
Peptide B name
DNA primase large subunit
Peptide A accession
P49643
Peptide B accession
P49643
Peptide A residue number
449
Peptide B residue number
449
Ligandability
5dqo D 367 D 424
A redox-regulated disulphide may form within DNA primase large subunit between cysteines 367 and 424. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
5dqo
Structure name
crystal structure of y347f mutant of human primase p58 iron-sulfur cluster domain
Structure deposition date
2015-09-15
Thiol separation (Å)
5
Half-sphere exposure sum ?
78
Minimum pKa ?
14
% buried
100
Peptide accession
P49643
Residue number A
367
Residue number B
424
Peptide name
DNA primase large subunit
Ligandability
Cysteine 367 of DNA primase large subunit
Cysteine 424 of DNA primase large subunit
3l9q B 287 B 384
A redox-regulated disulphide may form within DNA primase large subunit between cysteines 287 and 384. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
3l9q
Structure name
crystal structure of human polymerase alpha-primase p58 iron-sulfur cluster domain
Structure deposition date
2010-01-05
Thiol separation (Å)
6
Half-sphere exposure sum ?
86
Minimum pKa ?
12
% buried
100
Peptide accession
P49643
Residue number A
287
Residue number B
384
Peptide name
DNA primase large subunit
Ligandability
Cysteine 287 of DNA primase large subunit
Cysteine 384 of DNA primase large subunit
5dqo D 367 D 384
A redox-regulated disulphide may form within DNA primase large subunit between cysteines 367 and 384. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
5dqo
Structure name
crystal structure of y347f mutant of human primase p58 iron-sulfur cluster domain
Structure deposition date
2015-09-15
Thiol separation (Å)
7
Half-sphere exposure sum ?
77
Minimum pKa ?
11
% buried
98
Peptide accession
P49643
Residue number A
367
Residue number B
384
Peptide name
DNA primase large subunit
Ligandability
Cysteine 367 of DNA primase large subunit
Cysteine 384 of DNA primase large subunit
5dqo D 287 D 367
A redox-regulated disulphide may form within DNA primase large subunit between cysteines 287 and 367. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
5dqo
Structure name
crystal structure of y347f mutant of human primase p58 iron-sulfur cluster domain
Structure deposition date
2015-09-15
Thiol separation (Å)
7
Half-sphere exposure sum ?
79
Minimum pKa ?
13
% buried
100
Peptide accession
P49643
Residue number A
287
Residue number B
367
Peptide name
DNA primase large subunit
Ligandability
Cysteine 287 of DNA primase large subunit
Cysteine 367 of DNA primase large subunit
5exr B 287 B 424
A redox-regulated disulphide may form within DNA primase large subunit between cysteines 287 and 424. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
5exr
Structure name
crystal structure of human primosome
Structure deposition date
2015-11-24
Thiol separation (Å)
6
Half-sphere exposure sum ?
85
Minimum pKa ?
14
% buried
100
Peptide accession
P49643
Residue number A
287
Residue number B
424
Peptide name
DNA primase large subunit
Ligandability
Cysteine 287 of DNA primase large subunit
Cysteine 424 of DNA primase large subunit
6dhw A 384 A 424
A redox-regulated disulphide may form within DNA primase large subunit between cysteines 384 and 424. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
6dhw
Structure name
crystal structure of primase iron-sulfur domain (266-457)
Structure deposition date
2018-05-21
Thiol separation (Å)
7
Half-sphere exposure sum ?
82
Minimum pKa ?
12
% buried
100
Peptide accession
P49643
Residue number A
384
Residue number B
424
Peptide name
DNA primase large subunit
Ligandability
Cysteine 384 of DNA primase large subunit
Cysteine 424 of DNA primase large subunit
5f0q B 424 B 437
A redox-regulated disulphide may form within DNA primase large subunit between cysteines 424 and 437. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
5f0q
Structure name
crystal structure of c-terminal domain of the human dna primase large subunit with bound dna template/rna primer
Structure deposition date
2015-11-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
67
Minimum pKa ?
11
% buried
64
Peptide accession
P49643
Residue number A
424
Residue number B
437
Peptide name
DNA primase large subunit
Ligandability
Cysteine 424 of DNA primase large subunit
Cysteine 437 of DNA primase large subunit
If this tool was useful for finding a disulphide, please cite: