Protein unc-13 homolog A
Intermolecular
Cysteine 5 and cysteine 95 of Regulating synaptic membrane exocytosis protein 2
Cysteine 5 and cysteine 116 of Regulating synaptic membrane exocytosis protein 2
Intramolecular
Cysteine 593 and cysteine 612
Cysteine 593 and cysteine 596
Cysteine 600 and cysteine 616
Cysteine 576 and cysteine 604
Cysteine 580 and cysteine 604
Cysteine 576 and cysteine 579
Cysteine 1262 and cysteine 1375
Cysteine 593 and cysteine 600
More...Cysteine 604 and cysteine 608
Cysteine 579 and cysteine 604
Cysteine 579 and cysteine 600
Cysteine 596 and cysteine 600
Cysteine 1257 and cysteine 1266
Cysteine 1008 and cysteine 1012
2cjs A 5 C 95
A redox-regulated disulphide may form between cysteine 5 of Protein unc-13 homolog A and cysteine 95 of Regulating synaptic membrane exocytosis protein 2. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
2cjs
Structure name
structural basis for a munc13-1 homodimer - munc13-1 - rim heterodimer switch: c2-domains as versatile protein-protein interaction modules
Structure deposition date
2006-04-06
Thiol separation (Å)
10
Half-sphere exposure sum ?
60
Minimum pKa ?
7
% buried
57
Peptide A name
Protein unc-13 homolog A
Peptide B name
Regulating synaptic membrane exocytosis protein 2
Peptide A accession
Q62768
Peptide B accession
Q9JIS1
Peptide A residue number
5
Peptide B residue number
95
Ligandability
Cysteine 5 of Protein unc-13 homolog A
Cysteine 95 of Regulating synaptic membrane exocytosis protein 2
2cjs A 5 C 116
A redox-regulated disulphide may form between cysteine 5 of Protein unc-13 homolog A and cysteine 116 of Regulating synaptic membrane exocytosis protein 2. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
35
PDB code
2cjs
Structure name
structural basis for a munc13-1 homodimer - munc13-1 - rim heterodimer switch: c2-domains as versatile protein-protein interaction modules
Structure deposition date
2006-04-06
Thiol separation (Å)
8
Half-sphere exposure sum ?
82
Minimum pKa ?
12
% buried
74
Peptide A name
Protein unc-13 homolog A
Peptide B name
Regulating synaptic membrane exocytosis protein 2
Peptide A accession
Q62768
Peptide B accession
Q9JIS1
Peptide A residue number
5
Peptide B residue number
116
Ligandability
Cysteine 5 of Protein unc-13 homolog A
Cysteine 116 of Regulating synaptic membrane exocytosis protein 2
7t7v A 69 A 88
A redox-regulated disulphide may form within Protein unc-13 homolog A between cysteines 593 and 612 (69 and 88 respectively in this structure).
Details
Redox score ?
93
PDB code
7t7v
Structure name
munc13-1 c1-c2b-mun-c2c lateral conformation on lipid bilayer surface
Structure deposition date
2021-12-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
65
Minimum pKa ?
0
% buried
59
Peptide accession
Q4KUS2
Residue number A
593
Residue number B
612
Peptide name
Protein unc-13 homolog A
Ligandability
Cysteine 593 of Protein unc-13 homolog A
Cysteine 612 of Protein unc-13 homolog A
7t7r B 69 B 72
A redox-regulated disulphide may form within Protein unc-13 homolog A between cysteines 593 and 596 (69 and 72 respectively in this structure).
Details
Redox score ?
83
PDB code
7t7r
Structure name
structure of munc13-1 c1-c2b-mun-c2c trimer between lipid bilayers
Structure deposition date
2021-12-15
Thiol separation (Å)
3
Half-sphere exposure sum ?
67
Minimum pKa ?
8
% buried
38
Peptide accession
Q4KUS2
Residue number A
593
Residue number B
596
Peptide name
Protein unc-13 homolog A
Ligandability
Cysteine 593 of Protein unc-13 homolog A
Cysteine 596 of Protein unc-13 homolog A
5ue8 B 600 B 616
A redox-regulated disulphide may form within Protein unc-13 homolog A between cysteines 600 and 616.
Details
Redox score ?
82
PDB code
5ue8
Structure name
the crystal structure of munc13-1 c1c2bmun domain
Structure deposition date
2016-12-29
Thiol separation (Å)
3
Half-sphere exposure sum ?
55
Minimum pKa ?
10
% buried
45
Peptide accession
Q62768
Residue number A
600
Residue number B
616
Peptide name
Protein unc-13 homolog A
Ligandability
Cysteine 600 of Protein unc-13 homolog A
Cysteine 616 of Protein unc-13 homolog A
7t7x A 52 A 80
A redox-regulated disulphide may form within Protein unc-13 homolog A between cysteines 576 and 604 (52 and 80 respectively in this structure).
Details
Redox score ?
78
PDB code
7t7x
Structure name
munc13-1 c1-c2b-mun-c2c upright conformation spanning two lipid bilayers
Structure deposition date
2021-12-15
Thiol separation (Å)
3
Half-sphere exposure sum ?
59
Minimum pKa ?
10
% buried
48
Peptide accession
Q4KUS2
Residue number A
576
Residue number B
604
Peptide name
Protein unc-13 homolog A
Ligandability
Cysteine 576 of Protein unc-13 homolog A
Cysteine 604 of Protein unc-13 homolog A
5ue8 A 580 A 604
A redox-regulated disulphide may form within Protein unc-13 homolog A between cysteines 580 and 604.
Details
Redox score ?
71
PDB code
5ue8
Structure name
the crystal structure of munc13-1 c1c2bmun domain
Structure deposition date
2016-12-29
Thiol separation (Å)
5
Half-sphere exposure sum ?
64
Minimum pKa ?
7
% buried
44
Peptide accession
Q62768
Residue number A
580
Residue number B
604
Peptide name
Protein unc-13 homolog A
Ligandability
Cysteine 580 of Protein unc-13 homolog A
Cysteine 604 of Protein unc-13 homolog A
7t7v A 52 A 55
A redox-regulated disulphide may form within Protein unc-13 homolog A between cysteines 576 and 579 (52 and 55 respectively in this structure).
Details
Redox score ?
69
PDB code
7t7v
Structure name
munc13-1 c1-c2b-mun-c2c lateral conformation on lipid bilayer surface
Structure deposition date
2021-12-15
Thiol separation (Å)
3
Half-sphere exposure sum ?
74
Minimum pKa ?
12
% buried
nan
Peptide accession
Q4KUS2
Residue number A
576
Residue number B
579
Peptide name
Protein unc-13 homolog A
Ligandability
Cysteine 576 of Protein unc-13 homolog A
Cysteine 579 of Protein unc-13 homolog A
7t7v A 738 A 851
A redox-regulated disulphide may form within Protein unc-13 homolog A between cysteines 1262 and 1375 (738 and 851 respectively in this structure).
Details
Redox score ?
69
PDB code
7t7v
Structure name
munc13-1 c1-c2b-mun-c2c lateral conformation on lipid bilayer surface
Structure deposition date
2021-12-15
Thiol separation (Å)
3
Half-sphere exposure sum ?
88
Minimum pKa ?
9
% buried
100
Peptide accession
Q4KUS2
Residue number A
1262
Residue number B
1375
Peptide name
Protein unc-13 homolog A
Ligandability
Cysteine 1262 of Protein unc-13 homolog A
Cysteine 1375 of Protein unc-13 homolog A
7t7v A 69 A 76
A redox-regulated disulphide may form within Protein unc-13 homolog A between cysteines 593 and 600 (69 and 76 respectively in this structure).
Details
Redox score ?
65
PDB code
7t7v
Structure name
munc13-1 c1-c2b-mun-c2c lateral conformation on lipid bilayer surface
Structure deposition date
2021-12-15
Thiol separation (Å)
8
Half-sphere exposure sum ?
68
Minimum pKa ?
0
% buried
64
Peptide accession
Q4KUS2
Residue number A
593
Residue number B
600
Peptide name
Protein unc-13 homolog A
Ligandability
Cysteine 593 of Protein unc-13 homolog A
Cysteine 600 of Protein unc-13 homolog A
5ue8 A 604 A 608
A redox-regulated disulphide may form within Protein unc-13 homolog A between cysteines 604 and 608. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
57
PDB code
5ue8
Structure name
the crystal structure of munc13-1 c1c2bmun domain
Structure deposition date
2016-12-29
Thiol separation (Å)
6
Half-sphere exposure sum ?
58
Minimum pKa ?
11
% buried
30
Peptide accession
Q62768
Residue number A
604
Residue number B
608
Peptide name
Protein unc-13 homolog A
Ligandability
Cysteine 604 of Protein unc-13 homolog A
Cysteine 608 of Protein unc-13 homolog A
7t7v A 55 A 80
A redox-regulated disulphide may form within Protein unc-13 homolog A between cysteines 579 and 604 (55 and 80 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
7t7v
Structure name
munc13-1 c1-c2b-mun-c2c lateral conformation on lipid bilayer surface
Structure deposition date
2021-12-15
Thiol separation (Å)
3
Half-sphere exposure sum ?
68
Minimum pKa ?
21
% buried
nan
Peptide accession
Q4KUS2
Residue number A
579
Residue number B
604
Peptide name
Protein unc-13 homolog A
Ligandability
Cysteine 579 of Protein unc-13 homolog A
Cysteine 604 of Protein unc-13 homolog A
7t7r B 55 B 76
A redox-regulated disulphide may form within Protein unc-13 homolog A between cysteines 579 and 600 (55 and 76 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
7t7r
Structure name
structure of munc13-1 c1-c2b-mun-c2c trimer between lipid bilayers
Structure deposition date
2021-12-15
Thiol separation (Å)
8
Half-sphere exposure sum ?
70
Minimum pKa ?
7
% buried
48
Peptide accession
Q4KUS2
Residue number A
579
Residue number B
600
Peptide name
Protein unc-13 homolog A
Ligandability
Cysteine 579 of Protein unc-13 homolog A
Cysteine 600 of Protein unc-13 homolog A
7t7x A 72 A 76
A redox-regulated disulphide may form within Protein unc-13 homolog A between cysteines 596 and 600 (72 and 76 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
7t7x
Structure name
munc13-1 c1-c2b-mun-c2c upright conformation spanning two lipid bilayers
Structure deposition date
2021-12-15
Thiol separation (Å)
8
Half-sphere exposure sum ?
76
Minimum pKa ?
12
% buried
54
Peptide accession
Q4KUS2
Residue number A
596
Residue number B
600
Peptide name
Protein unc-13 homolog A
Ligandability
Cysteine 596 of Protein unc-13 homolog A
Cysteine 600 of Protein unc-13 homolog A
5ue8 B 1257 B 1266
A redox-regulated disulphide may form within Protein unc-13 homolog A between cysteines 1257 and 1266. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
5ue8
Structure name
the crystal structure of munc13-1 c1c2bmun domain
Structure deposition date
2016-12-29
Thiol separation (Å)
9
Half-sphere exposure sum ?
72
Minimum pKa ?
11
% buried
73
Peptide accession
Q62768
Residue number A
1257
Residue number B
1266
Peptide name
Protein unc-13 homolog A
Ligandability
Cysteine 1257 of Protein unc-13 homolog A
Cysteine 1266 of Protein unc-13 homolog A
7t7r B 484 B 488
A redox-regulated disulphide may form within Protein unc-13 homolog A between cysteines 1008 and 1012 (484 and 488 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
7t7r
Structure name
structure of munc13-1 c1-c2b-mun-c2c trimer between lipid bilayers
Structure deposition date
2021-12-15
Thiol separation (Å)
9
Half-sphere exposure sum ?
62
Minimum pKa ?
10
% buried
70
Peptide accession
Q4KUS2
Residue number A
1008
Residue number B
1012
Peptide name
Protein unc-13 homolog A
Ligandability
Cysteine 1008 of Protein unc-13 homolog A
Cysteine 1012 of Protein unc-13 homolog A
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