NACHT, LRR and PYD domains-containing protein 1
Intermolecular
Cysteine 844 of Dipeptidyl peptidase 9 and cysteine 1288 L
Intramolecular
Cysteine 910 and cysteine 911
Cysteine 886 and cysteine 910
Cysteine 854 and cysteine 904
Cysteine 886 and cysteine 911
Cysteine 911 and cysteine 943
Cysteine 904 and cysteine 910
Cysteine 854 and cysteine 886
6x6a D 844 F 1288
A redox-regulated disulphide may form between cysteine 844 of Dipeptidyl peptidase 9 and cysteine 1288 of NACHT, LRR and PYD domains-containing protein 1. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
31
PDB code
6x6a
Structure name
cryo-em structure of nlrp1-dpp9 complex
Structure deposition date
2020-05-27
Thiol separation (Å)
10
Half-sphere exposure sum ?
61
Minimum pKa ?
12
% buried
88
Peptide A name
Dipeptidyl peptidase 9
Peptide B name
NACHT, LRR and PYD domains-containing protein 1
Peptide A accession
Q86TI2
Peptide B accession
Q9C000
Peptide A residue number
844
Peptide B residue number
1288
Ligandability
Cysteine 844 of Dipeptidyl peptidase 9
Cysteine 1288 of NACHT, LRR and PYD domains-containing protein 1
4im6 A 910 A 911
A redox-regulated disulphide may form within NACHT, LRR and PYD domains-containing protein 1 between cysteines 910 and 911.
Details
Redox score ?
72
PDB code
4im6
Structure name
lrr domain from human nlrp1
Structure deposition date
2013-01-02
Thiol separation (Å)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
8
% buried
70
Peptide accession
Q9C000
Residue number A
910
Residue number B
911
Peptide name
NACHT, LRR and PYD domains-containing protein 1
Ligandability
Cysteine 910 of NACHT, LRR and PYD domains-containing protein 1
Cysteine 911 of NACHT, LRR and PYD domains-containing protein 1
4im6 A 886 A 910
A redox-regulated disulphide may form within NACHT, LRR and PYD domains-containing protein 1 between cysteines 886 and 910. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
4im6
Structure name
lrr domain from human nlrp1
Structure deposition date
2013-01-02
Thiol separation (Å)
7
Half-sphere exposure sum ?
67
Minimum pKa ?
12
% buried
83
Peptide accession
Q9C000
Residue number A
886
Residue number B
910
Peptide name
NACHT, LRR and PYD domains-containing protein 1
Ligandability
Cysteine 886 of NACHT, LRR and PYD domains-containing protein 1
Cysteine 910 of NACHT, LRR and PYD domains-containing protein 1
4im6 A 854 A 904
A redox-regulated disulphide may form within NACHT, LRR and PYD domains-containing protein 1 between cysteines 854 and 904. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
4im6
Structure name
lrr domain from human nlrp1
Structure deposition date
2013-01-02
Thiol separation (Å)
8
Half-sphere exposure sum ?
73
Minimum pKa ?
12
% buried
78
Peptide accession
Q9C000
Residue number A
854
Residue number B
904
Peptide name
NACHT, LRR and PYD domains-containing protein 1
Ligandability
Cysteine 854 of NACHT, LRR and PYD domains-containing protein 1
Cysteine 904 of NACHT, LRR and PYD domains-containing protein 1
4im6 A 886 A 911
A redox-regulated disulphide may form within NACHT, LRR and PYD domains-containing protein 1 between cysteines 886 and 911. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
4im6
Structure name
lrr domain from human nlrp1
Structure deposition date
2013-01-02
Thiol separation (Å)
9
Half-sphere exposure sum ?
66
Minimum pKa ?
8
% buried
82
Peptide accession
Q9C000
Residue number A
886
Residue number B
911
Peptide name
NACHT, LRR and PYD domains-containing protein 1
Ligandability
Cysteine 886 of NACHT, LRR and PYD domains-containing protein 1
Cysteine 911 of NACHT, LRR and PYD domains-containing protein 1
4im6 A 911 A 943
A redox-regulated disulphide may form within NACHT, LRR and PYD domains-containing protein 1 between cysteines 911 and 943. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
4im6
Structure name
lrr domain from human nlrp1
Structure deposition date
2013-01-02
Thiol separation (Å)
10
Half-sphere exposure sum ?
67
Minimum pKa ?
8
% buried
70
Peptide accession
Q9C000
Residue number A
911
Residue number B
943
Peptide name
NACHT, LRR and PYD domains-containing protein 1
Ligandability
Cysteine 911 of NACHT, LRR and PYD domains-containing protein 1
Cysteine 943 of NACHT, LRR and PYD domains-containing protein 1
4im6 A 904 A 910
A redox-regulated disulphide may form within NACHT, LRR and PYD domains-containing protein 1 between cysteines 904 and 910. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
36
PDB code
4im6
Structure name
lrr domain from human nlrp1
Structure deposition date
2013-01-02
Thiol separation (Å)
10
Half-sphere exposure sum ?
70
Minimum pKa ?
12
% buried
72
Peptide accession
Q9C000
Residue number A
904
Residue number B
910
Peptide name
NACHT, LRR and PYD domains-containing protein 1
Ligandability
Cysteine 904 of NACHT, LRR and PYD domains-containing protein 1
Cysteine 910 of NACHT, LRR and PYD domains-containing protein 1
4im6 A 854 A 886
A redox-regulated disulphide may form within NACHT, LRR and PYD domains-containing protein 1 between cysteines 854 and 886. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
31
PDB code
4im6
Structure name
lrr domain from human nlrp1
Structure deposition date
2013-01-02
Thiol separation (Å)
10
Half-sphere exposure sum ?
71
Minimum pKa ?
12
% buried
88
Peptide accession
Q9C000
Residue number A
854
Residue number B
886
Peptide name
NACHT, LRR and PYD domains-containing protein 1
Ligandability
Cysteine 854 of NACHT, LRR and PYD domains-containing protein 1
Cysteine 886 of NACHT, LRR and PYD domains-containing protein 1
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