Cell cycle checkpoint protein RAD1
Intermolecular
Cysteine 200 of Checkpoint protein HUS1 and cysteine 132
Cysteine 200 of Checkpoint protein HUS1 and cysteine 92
Intramolecular
Cysteine 58 and cysteine 272
Cysteine 92 and cysteine 132
Cysteine 148 and cysteine 272
Cysteine 271 and cysteine 272
Cysteine 58 and cysteine 271
Cysteine 58 and cysteine 148
Cysteine 42 and cysteine 111
6j8y B 200 C 132
A redox-regulated disulphide may form between cysteine 200 of Checkpoint protein HUS1 and cysteine 132 of Cell cycle checkpoint protein RAD1. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
35
PDB code
6j8y
Structure name
crystal structure of the human rad9-hus1-rad1-rhino complex
Structure deposition date
2019-01-21
Thiol separation (Å)
10
Half-sphere exposure sum ?
70
Minimum pKa ?
9
% buried
62
Peptide A name
Checkpoint protein HUS1
Peptide B name
Cell cycle checkpoint protein RAD1
Peptide A accession
O60921
Peptide B accession
O60671
Peptide A residue number
200
Peptide B residue number
132
Ligandability
Cysteine 200 of Checkpoint protein HUS1
Cysteine 132 of Cell cycle checkpoint protein RAD1
6j8y B 200 C 92
A redox-regulated disulphide may form between cysteine 200 of Checkpoint protein HUS1 and cysteine 92 of Cell cycle checkpoint protein RAD1. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
30
PDB code
6j8y
Structure name
crystal structure of the human rad9-hus1-rad1-rhino complex
Structure deposition date
2019-01-21
Thiol separation (Å)
10
Half-sphere exposure sum ?
76
Minimum pKa ?
10
% buried
62
Peptide A name
Checkpoint protein HUS1
Peptide B name
Cell cycle checkpoint protein RAD1
Peptide A accession
O60921
Peptide B accession
O60671
Peptide A residue number
200
Peptide B residue number
92
Ligandability
Cysteine 200 of Checkpoint protein HUS1
Cysteine 92 of Cell cycle checkpoint protein RAD1
3g65 B 58 B 272
A redox-regulated disulphide may form within Cell cycle checkpoint protein RAD1 between cysteines 58 and 272.
Details
Redox score ?
79
PDB code
3g65
Structure name
crystal structure of the human rad9-rad1-hus1 dna damage checkpoint complex
Structure deposition date
2009-02-06
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
6
% buried
42
Peptide accession
O60671
Residue number A
58
Residue number B
272
Peptide name
Cell cycle checkpoint protein RAD1
Ligandability
Cysteine 58 of Cell cycle checkpoint protein RAD1
Cysteine 272 of Cell cycle checkpoint protein RAD1
3g65 B 92 B 132
A redox-regulated disulphide may form within Cell cycle checkpoint protein RAD1 between cysteines 92 and 132.
Details
Redox score ?
70
PDB code
3g65
Structure name
crystal structure of the human rad9-rad1-hus1 dna damage checkpoint complex
Structure deposition date
2009-02-06
Thiol separation (Å)
4
Half-sphere exposure sum ?
87
Minimum pKa ?
8
% buried
100
Peptide accession
O60671
Residue number A
92
Residue number B
132
Peptide name
Cell cycle checkpoint protein RAD1
Ligandability
Cysteine 92 of Cell cycle checkpoint protein RAD1
Cysteine 132 of Cell cycle checkpoint protein RAD1
3ggr C 148 C 272
A redox-regulated disulphide may form within Cell cycle checkpoint protein RAD1 between cysteines 148 and 272. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
59
PDB code
3ggr
Structure name
crystal structure of the human rad9-hus1-rad1 complex
Structure deposition date
2009-03-02
Thiol separation (Å)
6
Half-sphere exposure sum ?
62
Minimum pKa ?
10
% buried
31
Peptide accession
O60671
Residue number A
148
Residue number B
272
Peptide name
Cell cycle checkpoint protein RAD1
Ligandability
Cysteine 148 of Cell cycle checkpoint protein RAD1
Cysteine 272 of Cell cycle checkpoint protein RAD1
6j8y C 271 C 272
A redox-regulated disulphide may form within Cell cycle checkpoint protein RAD1 between cysteines 271 and 272. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
57
PDB code
6j8y
Structure name
crystal structure of the human rad9-hus1-rad1-rhino complex
Structure deposition date
2019-01-21
Thiol separation (Å)
5
Half-sphere exposure sum ?
77
Minimum pKa ?
12
% buried
nan
Peptide accession
O60671
Residue number A
271
Residue number B
272
Peptide name
Cell cycle checkpoint protein RAD1
Ligandability
Cysteine 271 of Cell cycle checkpoint protein RAD1
Cysteine 272 of Cell cycle checkpoint protein RAD1
6j8y C 58 C 271
A redox-regulated disulphide may form within Cell cycle checkpoint protein RAD1 between cysteines 58 and 271. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
52
PDB code
6j8y
Structure name
crystal structure of the human rad9-hus1-rad1-rhino complex
Structure deposition date
2019-01-21
Thiol separation (Å)
6
Half-sphere exposure sum ?
70
Minimum pKa ?
12
% buried
nan
Peptide accession
O60671
Residue number A
58
Residue number B
271
Peptide name
Cell cycle checkpoint protein RAD1
Ligandability
Cysteine 58 of Cell cycle checkpoint protein RAD1
Cysteine 271 of Cell cycle checkpoint protein RAD1
3ggr C 58 C 148
A redox-regulated disulphide may form within Cell cycle checkpoint protein RAD1 between cysteines 58 and 148. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
3ggr
Structure name
crystal structure of the human rad9-hus1-rad1 complex
Structure deposition date
2009-03-02
Thiol separation (Å)
10
Half-sphere exposure sum ?
53
Minimum pKa ?
10
% buried
26
Peptide accession
O60671
Residue number A
58
Residue number B
148
Peptide name
Cell cycle checkpoint protein RAD1
Ligandability
Cysteine 58 of Cell cycle checkpoint protein RAD1
Cysteine 148 of Cell cycle checkpoint protein RAD1
3ggr C 42 C 111
A redox-regulated disulphide may form within Cell cycle checkpoint protein RAD1 between cysteines 42 and 111. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
3ggr
Structure name
crystal structure of the human rad9-hus1-rad1 complex
Structure deposition date
2009-03-02
Thiol separation (Å)
8
Half-sphere exposure sum ?
68
Minimum pKa ?
11
% buried
80
Peptide accession
O60671
Residue number A
42
Residue number B
111
Peptide name
Cell cycle checkpoint protein RAD1
Ligandability
Cysteine 42 of Cell cycle checkpoint protein RAD1
Cysteine 111 of Cell cycle checkpoint protein RAD1
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