Protein-arginine deiminase type-3
Intermolecular
Cysteine 564 and cysteine 125
Intramolecular
Cysteine 173 and cysteine 223
Cysteine 19 and cysteine 114
Cysteine 311 and cysteine 337
Cysteine 611 and cysteine 612
Cysteine 161 and cysteine 173
Cysteine 161 and cysteine 167
Cysteine 610 and cysteine 611
Cysteine 121 and cysteine 125
Cysteine 332 and cysteine 651
More...Cysteine 506 and cysteine 612
Cysteine 610 and cysteine 612
Cysteine 496 and cysteine 612
Cysteine 496 and cysteine 611
Cysteine 154 and cysteine 167
7dan C 564 B 125
A redox-regulated disulphide may form between two units of Protein-arginine deiminase type-3 at cysteines 564 and 125. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
7dan
Structure name
structure of the ca2+-bound wild-type peptidylarginine deiminase type iii (pad3)
Structure deposition date
2020-10-16
Thiol separation (Å)
10
Half-sphere exposure sum ?
36
Minimum pKa ?
9
% buried
4
Peptide A name
Protein-arginine deiminase type-3
Peptide B name
Protein-arginine deiminase type-3
Peptide A accession
Q9ULW8
Peptide B accession
Q9ULW8
Peptide A residue number
564
Peptide B residue number
125
Ligandability
Cysteine 564 of Protein-arginine deiminase type-3
Cysteine 125 of Protein-arginine deiminase type-3
7d4y B 173 B 223
A redox-regulated disulphide may form within Protein-arginine deiminase type-3 between cysteines 173 and 223.
Details
Redox score ?
71
PDB code
7d4y
Structure name
structure of human wild-type peptidylarginine deiminase type iii (pad3)
Structure deposition date
2020-09-24
Thiol separation (Å)
6
Half-sphere exposure sum ?
nan
Minimum pKa ?
10
% buried
2
Peptide accession
Q9ULW8
Residue number A
173
Residue number B
223
Peptide name
Protein-arginine deiminase type-3
Ligandability
Cysteine 173 of Protein-arginine deiminase type-3
Cysteine 223 of Protein-arginine deiminase type-3
7d8n A 19 A 114
A redox-regulated disulphide may form within Protein-arginine deiminase type-3 between cysteines 19 and 114.
Details
Redox score ?
68
PDB code
7d8n
Structure name
structure of the inactive form of wild-type peptidylarginine deiminase type iii (pad3) crystallized under the condition with high concentrations of ca2+
Structure deposition date
2020-10-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
85
Minimum pKa ?
8
% buried
71
Peptide accession
Q9ULW8
Residue number A
19
Residue number B
114
Peptide name
Protein-arginine deiminase type-3
Ligandability
Cysteine 19 of Protein-arginine deiminase type-3
Cysteine 114 of Protein-arginine deiminase type-3
7d8n B 311 B 337
A redox-regulated disulphide may form within Protein-arginine deiminase type-3 between cysteines 311 and 337.
Details
Redox score ?
66
PDB code
7d8n
Structure name
structure of the inactive form of wild-type peptidylarginine deiminase type iii (pad3) crystallized under the condition with high concentrations of ca2+
Structure deposition date
2020-10-08
Thiol separation (Å)
5
Half-sphere exposure sum ?
54
Minimum pKa ?
10
% buried
38
Peptide accession
Q9ULW8
Residue number A
311
Residue number B
337
Peptide name
Protein-arginine deiminase type-3
Ligandability
Cysteine 311 of Protein-arginine deiminase type-3
Cysteine 337 of Protein-arginine deiminase type-3
7d5v B 611 B 612
A redox-regulated disulphide may form within Protein-arginine deiminase type-3 between cysteines 611 and 612. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
58
PDB code
7d5v
Structure name
structure of the c646a mutant of peptidylarginine deiminase type iii (pad3)
Structure deposition date
2020-09-28
Thiol separation (Å)
6
Half-sphere exposure sum ?
59
Minimum pKa ?
10
% buried
74
Peptide accession
Q9ULW8
Residue number A
611
Residue number B
612
Peptide name
Protein-arginine deiminase type-3
Ligandability
Cysteine 611 of Protein-arginine deiminase type-3
Cysteine 612 of Protein-arginine deiminase type-3
7d8n B 161 B 173
A redox-regulated disulphide may form within Protein-arginine deiminase type-3 between cysteines 161 and 173. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
7d8n
Structure name
structure of the inactive form of wild-type peptidylarginine deiminase type iii (pad3) crystallized under the condition with high concentrations of ca2+
Structure deposition date
2020-10-08
Thiol separation (Å)
9
Half-sphere exposure sum ?
45
Minimum pKa ?
9
% buried
23
Peptide accession
Q9ULW8
Residue number A
161
Residue number B
173
Peptide name
Protein-arginine deiminase type-3
Ligandability
Cysteine 161 of Protein-arginine deiminase type-3
Cysteine 173 of Protein-arginine deiminase type-3
7d56 C 161 C 167
A redox-regulated disulphide may form within Protein-arginine deiminase type-3 between cysteines 161 and 167. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
7d56
Structure name
structure of the peptidylarginine deiminase type iii (pad3) in complex with cl-amidine
Structure deposition date
2020-09-25
Thiol separation (Å)
9
Half-sphere exposure sum ?
46
Minimum pKa ?
10
% buried
16
Peptide accession
Q9ULW8
Residue number A
161
Residue number B
167
Peptide name
Protein-arginine deiminase type-3
Ligandability
Cysteine 161 of Protein-arginine deiminase type-3
Cysteine 167 of Protein-arginine deiminase type-3
7d5v A 610 A 611
A redox-regulated disulphide may form within Protein-arginine deiminase type-3 between cysteines 610 and 611. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
7d5v
Structure name
structure of the c646a mutant of peptidylarginine deiminase type iii (pad3)
Structure deposition date
2020-09-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
46
Minimum pKa ?
9
% buried
36
Peptide accession
Q9ULW8
Residue number A
610
Residue number B
611
Peptide name
Protein-arginine deiminase type-3
Ligandability
Cysteine 610 of Protein-arginine deiminase type-3
Cysteine 611 of Protein-arginine deiminase type-3
7d4y B 121 B 125
A redox-regulated disulphide may form within Protein-arginine deiminase type-3 between cysteines 121 and 125. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
7d4y
Structure name
structure of human wild-type peptidylarginine deiminase type iii (pad3)
Structure deposition date
2020-09-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
62
Minimum pKa ?
9
% buried
54
Peptide accession
Q9ULW8
Residue number A
121
Residue number B
125
Peptide name
Protein-arginine deiminase type-3
Ligandability
Cysteine 121 of Protein-arginine deiminase type-3
Cysteine 125 of Protein-arginine deiminase type-3
7dan A 332 A 651
A redox-regulated disulphide may form within Protein-arginine deiminase type-3 between cysteines 332 and 651. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
7dan
Structure name
structure of the ca2+-bound wild-type peptidylarginine deiminase type iii (pad3)
Structure deposition date
2020-10-16
Thiol separation (Å)
8
Half-sphere exposure sum ?
69
Minimum pKa ?
10
% buried
60
Peptide accession
Q9ULW8
Residue number A
332
Residue number B
651
Peptide name
Protein-arginine deiminase type-3
Ligandability
Cysteine 332 of Protein-arginine deiminase type-3
Cysteine 651 of Protein-arginine deiminase type-3
7d4y B 506 B 612
A redox-regulated disulphide may form within Protein-arginine deiminase type-3 between cysteines 506 and 612. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
7d4y
Structure name
structure of human wild-type peptidylarginine deiminase type iii (pad3)
Structure deposition date
2020-09-24
Thiol separation (Å)
10
Half-sphere exposure sum ?
47
Minimum pKa ?
9
% buried
33
Peptide accession
Q9ULW8
Residue number A
506
Residue number B
612
Peptide name
Protein-arginine deiminase type-3
Ligandability
Cysteine 506 of Protein-arginine deiminase type-3
Cysteine 612 of Protein-arginine deiminase type-3
7d5v B 610 B 612
A redox-regulated disulphide may form within Protein-arginine deiminase type-3 between cysteines 610 and 612. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
7d5v
Structure name
structure of the c646a mutant of peptidylarginine deiminase type iii (pad3)
Structure deposition date
2020-09-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
55
Minimum pKa ?
11
% buried
37
Peptide accession
Q9ULW8
Residue number A
610
Residue number B
612
Peptide name
Protein-arginine deiminase type-3
Ligandability
Cysteine 610 of Protein-arginine deiminase type-3
Cysteine 612 of Protein-arginine deiminase type-3
7dan A 496 A 612
A redox-regulated disulphide may form within Protein-arginine deiminase type-3 between cysteines 496 and 612. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
7dan
Structure name
structure of the ca2+-bound wild-type peptidylarginine deiminase type iii (pad3)
Structure deposition date
2020-10-16
Thiol separation (Å)
8
Half-sphere exposure sum ?
68
Minimum pKa ?
12
% buried
86
Peptide accession
Q9ULW8
Residue number A
496
Residue number B
612
Peptide name
Protein-arginine deiminase type-3
Ligandability
Cysteine 496 of Protein-arginine deiminase type-3
Cysteine 612 of Protein-arginine deiminase type-3
6ce1 A 496 A 611
A redox-regulated disulphide may form within Protein-arginine deiminase type-3 between cysteines 496 and 611. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
6ce1
Structure name
crystal structure of peptidyl arginine deiminase type iii (padi3)
Structure deposition date
2018-02-10
Thiol separation (Å)
10
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9ULW8
Residue number A
496
Residue number B
611
Peptide name
Protein-arginine deiminase type-3
Ligandability
Cysteine 496 of Protein-arginine deiminase type-3
Cysteine 611 of Protein-arginine deiminase type-3
7d56 C 154 C 167
A redox-regulated disulphide may form within Protein-arginine deiminase type-3 between cysteines 154 and 167. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
35
PDB code
7d56
Structure name
structure of the peptidylarginine deiminase type iii (pad3) in complex with cl-amidine
Structure deposition date
2020-09-25
Thiol separation (Å)
9
Half-sphere exposure sum ?
66
Minimum pKa ?
10
% buried
64
Peptide accession
Q9ULW8
Residue number A
154
Residue number B
167
Peptide name
Protein-arginine deiminase type-3
Ligandability
Cysteine 154 of Protein-arginine deiminase type-3
Cysteine 167 of Protein-arginine deiminase type-3
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