E3 ubiquitin-protein ligase RNF31
Intermolecular
Cysteine 59 and cysteine 59
Cysteine 551 and cysteine 551
Cysteine 874 and cysteine 885
Cysteine 893 and cysteine 885
Intramolecular
Cysteine 719 and cysteine 747
Cysteine 799 and cysteine 817
Cysteine 874 and cysteine 890
Cysteine 799 and cysteine 802
Cysteine 911 and cysteine 916
Cysteine 356 and cysteine 370
More...Cysteine 359 and cysteine 370
Cysteine 871 and cysteine 893
Cysteine 890 and cysteine 893
Cysteine 825 and cysteine 841
Cysteine 356 and cysteine 373
Cysteine 370 and cysteine 373
Cysteine 356 and cysteine 359
Cysteine 717 and cysteine 747
Cysteine 828 and cysteine 841
Cysteine 359 and cysteine 373
Cysteine 699 and cysteine 702
Cysteine 871 and cysteine 890
Cysteine 699 and cysteine 722
Cysteine 722 and cysteine 725
Cysteine 717 and cysteine 719
Cysteine 871 and cysteine 874
Cysteine 969 and cysteine 986
Cysteine 504 and cysteine 551
Cysteine 717 and cysteine 744
Cysteine 825 and cysteine 828
Cysteine 874 and cysteine 893
Cysteine 969 and cysteine 998
Cysteine 799 and cysteine 820
Cysteine 719 and cysteine 744
Cysteine 702 and cysteine 725
Cysteine 986 and cysteine 998
Cysteine 744 and cysteine 747
Cysteine 702 and cysteine 722
Cysteine 901 and cysteine 930
Cysteine 898 and cysteine 930
4oyj G 59 H 59
A redox-regulated disulphide may form between two units of E3 ubiquitin-protein ligase RNF31 at cysteines 59 and 59.
Details
Redox score ?
83
PDB code
4oyj
Structure name
structure of the apo hoip pub domain
Structure deposition date
2014-02-12
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide A name
E3 ubiquitin-protein ligase RNF31
Peptide B name
E3 ubiquitin-protein ligase RNF31
Peptide A accession
Q96EP0
Peptide B accession
Q96EP0
Peptide A residue number
59
Peptide B residue number
59
Ligandability
7uyk A 551 B 551
A redox-regulated disulphide may form between two units of E3 ubiquitin-protein ligase RNF31 at cysteines 551 and 551.
Details
Redox score ?
66
PDB code
7uyk
Structure name
structure of rnf31 in complex with fp06655, a helicon polypeptide
Structure deposition date
2022-05-06
Thiol separation (Å)
5
Half-sphere exposure sum ?
76
Minimum pKa ?
9
% buried
88
Peptide A name
E3 ubiquitin-protein ligase RNF31
Peptide B name
E3 ubiquitin-protein ligase RNF31
Peptide A accession
Q96EP0
Peptide B accession
Q96EP0
Peptide A residue number
551
Peptide B residue number
551
Ligandability
6gzy A 874 B 885
A redox-regulated disulphide may form between two units of E3 ubiquitin-protein ligase RNF31 at cysteines 874 and 885.
Details
Redox score ?
66
PDB code
6gzy
Structure name
hoip-fragment5 complex
Structure deposition date
2018-07-05
Thiol separation (Å)
5
Half-sphere exposure sum ?
63
Minimum pKa ?
8
% buried
90
Peptide A name
E3 ubiquitin-protein ligase RNF31
Peptide B name
E3 ubiquitin-protein ligase RNF31
Peptide A accession
Q96EP0
Peptide B accession
Q96EP0
Peptide A residue number
874
Peptide B residue number
885
Ligandability
Cysteine 874 of E3 ubiquitin-protein ligase RNF31
Cysteine 885 of E3 ubiquitin-protein ligase RNF31
6gzy A 893 B 885
A redox-regulated disulphide may form between two units of E3 ubiquitin-protein ligase RNF31 at cysteines 893 and 885.
Details
Redox score ?
66
PDB code
6gzy
Structure name
hoip-fragment5 complex
Structure deposition date
2018-07-05
Thiol separation (Å)
5
Half-sphere exposure sum ?
64
Minimum pKa ?
8
% buried
90
Peptide A name
E3 ubiquitin-protein ligase RNF31
Peptide B name
E3 ubiquitin-protein ligase RNF31
Peptide A accession
Q96EP0
Peptide B accession
Q96EP0
Peptide A residue number
893
Peptide B residue number
885
Ligandability
Cysteine 893 of E3 ubiquitin-protein ligase RNF31
Cysteine 885 of E3 ubiquitin-protein ligase RNF31
7v8g D 719 D 747
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF31 between cysteines 719 and 747.
Details
Redox score ?
94
PDB code
7v8g
Structure name
crystal structure of hoip ring1 domain bound to ipah1
Structure deposition date
2021-08-23
Thiol separation (Å)
3
Half-sphere exposure sum ?
65
Minimum pKa ?
1
% buried
57
Peptide accession
Q96EP0
Residue number A
719
Residue number B
747
Peptide name
E3 ubiquitin-protein ligase RNF31
Ligandability
Cysteine 719 of E3 ubiquitin-protein ligase RNF31
Cysteine 747 of E3 ubiquitin-protein ligase RNF31
5edv A 799 A 817
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF31 between cysteines 799 and 817.
Details
Redox score ?
92
PDB code
5edv
Structure name
structure of the hoip-rbr/ubch5b~ubiquitin transfer complex
Structure deposition date
2015-10-22
Thiol separation (Å)
3
Half-sphere exposure sum ?
69
Minimum pKa ?
2
% buried
53
Peptide accession
Q96EP0
Residue number A
799
Residue number B
817
Peptide name
E3 ubiquitin-protein ligase RNF31
Ligandability
Cysteine 799 of E3 ubiquitin-protein ligase RNF31
Cysteine 817 of E3 ubiquitin-protein ligase RNF31
6kc6 K 874 K 890
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF31 between cysteines 874 and 890.
Details
Redox score ?
91
PDB code
6kc6
Structure name
hoip-hoipin8 complex
Structure deposition date
2019-06-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
44
Minimum pKa ?
5
% buried
0
Peptide accession
Q96EP0
Residue number A
874
Residue number B
890
Peptide name
E3 ubiquitin-protein ligase RNF31
Ligandability
Cysteine 874 of E3 ubiquitin-protein ligase RNF31
Cysteine 890 of E3 ubiquitin-protein ligase RNF31
5edv B 799 B 802
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF31 between cysteines 799 and 802.
Details
Redox score ?
90
PDB code
5edv
Structure name
structure of the hoip-rbr/ubch5b~ubiquitin transfer complex
Structure deposition date
2015-10-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
71
Minimum pKa ?
1
% buried
54
Peptide accession
Q96EP0
Residue number A
799
Residue number B
802
Peptide name
E3 ubiquitin-protein ligase RNF31
Ligandability
Cysteine 799 of E3 ubiquitin-protein ligase RNF31
Cysteine 802 of E3 ubiquitin-protein ligase RNF31
5edv A 911 A 916
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF31 between cysteines 911 and 916.
Details
Redox score ?
89
PDB code
5edv
Structure name
structure of the hoip-rbr/ubch5b~ubiquitin transfer complex
Structure deposition date
2015-10-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
39
Minimum pKa ?
8
% buried
2
Peptide accession
Q96EP0
Residue number A
911
Residue number B
916
Peptide name
E3 ubiquitin-protein ligase RNF31
Ligandability
Cysteine 911 of E3 ubiquitin-protein ligase RNF31
Cysteine 916 of E3 ubiquitin-protein ligase RNF31
7tv4 K 356 K 370
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF31 between cysteines 356 and 370.
Details
Redox score ?
89
PDB code
7tv4
Structure name
crystal structure of nemo cozi in complex with hoip nzf1 and linear diubiquitin
Structure deposition date
2022-02-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
5
% buried
0
Peptide accession
Q96EP0
Residue number A
356
Residue number B
370
Peptide name
E3 ubiquitin-protein ligase RNF31
Ligandability
Cysteine 356 of E3 ubiquitin-protein ligase RNF31
Cysteine 370 of E3 ubiquitin-protein ligase RNF31
4owf G 359 G 370
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF31 between cysteines 359 and 370.
Details
Redox score ?
89
PDB code
4owf
Structure name
crystal structure of the nemo cozi in complex with hoip nzf1 domain
Structure deposition date
2014-01-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
5
% buried
0
Peptide accession
Q96EP0
Residue number A
359
Residue number B
370
Peptide name
E3 ubiquitin-protein ligase RNF31
Ligandability
Cysteine 359 of E3 ubiquitin-protein ligase RNF31
Cysteine 370 of E3 ubiquitin-protein ligase RNF31
6kc5 B 871 B 893
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF31 between cysteines 871 and 893.
Details
Redox score ?
88
PDB code
6kc5
Structure name
hoip-hoipin1 complex
Structure deposition date
2019-06-27
Thiol separation (Å)
3
Half-sphere exposure sum ?
44
Minimum pKa ?
7
% buried
0
Peptide accession
Q96EP0
Residue number A
871
Residue number B
893
Peptide name
E3 ubiquitin-protein ligase RNF31
Ligandability
Cysteine 871 of E3 ubiquitin-protein ligase RNF31
Cysteine 893 of E3 ubiquitin-protein ligase RNF31
6sc6 A 890 A 893
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF31 between cysteines 890 and 893.
Details
Redox score ?
88
PDB code
6sc6
Structure name
dab3/hoip-rbr apo structure
Structure deposition date
2019-07-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
6
% buried
26
Peptide accession
Q96EP0
Residue number A
890
Residue number B
893
Peptide name
E3 ubiquitin-protein ligase RNF31
Ligandability
Cysteine 890 of E3 ubiquitin-protein ligase RNF31
Cysteine 893 of E3 ubiquitin-protein ligase RNF31
6sc5 A 825 A 841
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF31 between cysteines 825 and 841.
Details
Redox score ?
88
PDB code
6sc5
Structure name
dab3/hoip-rbr-ligand2
Structure deposition date
2019-07-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
3
% buried
32
Peptide accession
Q96EP0
Residue number A
825
Residue number B
841
Peptide name
E3 ubiquitin-protein ligase RNF31
Ligandability
Cysteine 825 of E3 ubiquitin-protein ligase RNF31
Cysteine 841 of E3 ubiquitin-protein ligase RNF31
4owf G 356 G 373
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF31 between cysteines 356 and 373.
Details
Redox score ?
87
PDB code
4owf
Structure name
crystal structure of the nemo cozi in complex with hoip nzf1 domain
Structure deposition date
2014-01-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
45
Minimum pKa ?
7
% buried
1
Peptide accession
Q96EP0
Residue number A
356
Residue number B
373
Peptide name
E3 ubiquitin-protein ligase RNF31
Ligandability
Cysteine 356 of E3 ubiquitin-protein ligase RNF31
Cysteine 373 of E3 ubiquitin-protein ligase RNF31
4owf G 370 G 373
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF31 between cysteines 370 and 373.
Details
Redox score ?
87
PDB code
4owf
Structure name
crystal structure of the nemo cozi in complex with hoip nzf1 domain
Structure deposition date
2014-01-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
5
% buried
1
Peptide accession
Q96EP0
Residue number A
370
Residue number B
373
Peptide name
E3 ubiquitin-protein ligase RNF31
Ligandability
Cysteine 370 of E3 ubiquitin-protein ligase RNF31
Cysteine 373 of E3 ubiquitin-protein ligase RNF31
7tv4 K 356 K 359
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF31 between cysteines 356 and 359.
Details
Redox score ?
87
PDB code
7tv4
Structure name
crystal structure of nemo cozi in complex with hoip nzf1 and linear diubiquitin
Structure deposition date
2022-02-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
42
Minimum pKa ?
5
% buried
0
Peptide accession
Q96EP0
Residue number A
356
Residue number B
359
Peptide name
E3 ubiquitin-protein ligase RNF31
Ligandability
Cysteine 356 of E3 ubiquitin-protein ligase RNF31
Cysteine 359 of E3 ubiquitin-protein ligase RNF31
5edv B 717 B 747
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF31 between cysteines 717 and 747.
Details
Redox score ?
85
PDB code
5edv
Structure name
structure of the hoip-rbr/ubch5b~ubiquitin transfer complex
Structure deposition date
2015-10-22
Thiol separation (Å)
3
Half-sphere exposure sum ?
42
Minimum pKa ?
9
% buried
12
Peptide accession
Q96EP0
Residue number A
717
Residue number B
747
Peptide name
E3 ubiquitin-protein ligase RNF31
Ligandability
Cysteine 717 of E3 ubiquitin-protein ligase RNF31
Cysteine 747 of E3 ubiquitin-protein ligase RNF31
6sc7 A 828 A 841
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF31 between cysteines 828 and 841.
Details
Redox score ?
83
PDB code
6sc7
Structure name
dab3/hoip-rbr-ligand3
Structure deposition date
2019-07-23
Thiol separation (Å)
3
Half-sphere exposure sum ?
55
Minimum pKa ?
8
% buried
26
Peptide accession
Q96EP0
Residue number A
828
Residue number B
841
Peptide name
E3 ubiquitin-protein ligase RNF31
Ligandability
Cysteine 828 of E3 ubiquitin-protein ligase RNF31
Cysteine 841 of E3 ubiquitin-protein ligase RNF31
7tv4 K 359 K 373
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF31 between cysteines 359 and 373.
Details
Redox score ?
83
PDB code
7tv4
Structure name
crystal structure of nemo cozi in complex with hoip nzf1 and linear diubiquitin
Structure deposition date
2022-02-03
Thiol separation (Å)
3
Half-sphere exposure sum ?
33
Minimum pKa ?
9
% buried
0
Peptide accession
Q96EP0
Residue number A
359
Residue number B
373
Peptide name
E3 ubiquitin-protein ligase RNF31
Ligandability
Cysteine 359 of E3 ubiquitin-protein ligase RNF31
Cysteine 373 of E3 ubiquitin-protein ligase RNF31
7v8f B 699 B 702
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF31 between cysteines 699 and 702.
Details
Redox score ?
83
PDB code
7v8f
Structure name
crystal structure of ube2l3 bound to hoip ring1 domain
Structure deposition date
2021-08-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
73
Minimum pKa ?
5
% buried
nan
Peptide accession
Q96EP0
Residue number A
699
Residue number B
702
Peptide name
E3 ubiquitin-protein ligase RNF31
Ligandability
Cysteine 699 of E3 ubiquitin-protein ligase RNF31
Cysteine 702 of E3 ubiquitin-protein ligase RNF31
5edv B 871 B 890
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF31 between cysteines 871 and 890.
Details
Redox score ?
83
PDB code
5edv
Structure name
structure of the hoip-rbr/ubch5b~ubiquitin transfer complex
Structure deposition date
2015-10-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
6
% buried
48
Peptide accession
Q96EP0
Residue number A
871
Residue number B
890
Peptide name
E3 ubiquitin-protein ligase RNF31
Ligandability
Cysteine 871 of E3 ubiquitin-protein ligase RNF31
Cysteine 890 of E3 ubiquitin-protein ligase RNF31
7v8g C 699 C 722
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF31 between cysteines 699 and 722.
Details
Redox score ?
82
PDB code
7v8g
Structure name
crystal structure of hoip ring1 domain bound to ipah1
Structure deposition date
2021-08-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
5
% buried
nan
Peptide accession
Q96EP0
Residue number A
699
Residue number B
722
Peptide name
E3 ubiquitin-protein ligase RNF31
Ligandability
Cysteine 699 of E3 ubiquitin-protein ligase RNF31
Cysteine 722 of E3 ubiquitin-protein ligase RNF31
7v8g D 722 D 725
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF31 between cysteines 722 and 725.
Details
Redox score ?
82
PDB code
7v8g
Structure name
crystal structure of hoip ring1 domain bound to ipah1
Structure deposition date
2021-08-23
Thiol separation (Å)
3
Half-sphere exposure sum ?
67
Minimum pKa ?
6
% buried
68
Peptide accession
Q96EP0
Residue number A
722
Residue number B
725
Peptide name
E3 ubiquitin-protein ligase RNF31
Ligandability
Cysteine 722 of E3 ubiquitin-protein ligase RNF31
Cysteine 725 of E3 ubiquitin-protein ligase RNF31
6sc7 A 717 A 719
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF31 between cysteines 717 and 719.
Details
Redox score ?
81
PDB code
6sc7
Structure name
dab3/hoip-rbr-ligand3
Structure deposition date
2019-07-23
Thiol separation (Å)
3
Half-sphere exposure sum ?
47
Minimum pKa ?
9
% buried
4
Peptide accession
Q96EP0
Residue number A
717
Residue number B
719
Peptide name
E3 ubiquitin-protein ligase RNF31
Ligandability
Cysteine 717 of E3 ubiquitin-protein ligase RNF31
Cysteine 719 of E3 ubiquitin-protein ligase RNF31
5edv A 871 A 874
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF31 between cysteines 871 and 874.
Details
Redox score ?
81
PDB code
5edv
Structure name
structure of the hoip-rbr/ubch5b~ubiquitin transfer complex
Structure deposition date
2015-10-22
Thiol separation (Å)
3
Half-sphere exposure sum ?
53
Minimum pKa ?
8
% buried
34
Peptide accession
Q96EP0
Residue number A
871
Residue number B
874
Peptide name
E3 ubiquitin-protein ligase RNF31
Ligandability
Cysteine 871 of E3 ubiquitin-protein ligase RNF31
Cysteine 874 of E3 ubiquitin-protein ligase RNF31
4ljp A 969 A 986
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF31 between cysteines 969 and 986.
Details
Redox score ?
81
PDB code
4ljp
Structure name
structure of an active ligase (hoip-h889a)/ubiquitin transfer complex
Structure deposition date
2013-07-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
6
% buried
44
Peptide accession
Q96EP0
Residue number A
969
Residue number B
986
Peptide name
E3 ubiquitin-protein ligase RNF31
Ligandability
Cysteine 969 of E3 ubiquitin-protein ligase RNF31
Cysteine 986 of E3 ubiquitin-protein ligase RNF31
4dbg B 504 B 551
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF31 between cysteines 504 and 551.
Details
Redox score ?
80
PDB code
4dbg
Structure name
crystal structure of hoil-1l-ubl complexed with a hoip-uba derivative
Structure deposition date
2012-01-15
Thiol separation (Å)
2
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96EP0
Residue number A
504
Residue number B
551
Peptide name
E3 ubiquitin-protein ligase RNF31
Ligandability
Cysteine 504 of E3 ubiquitin-protein ligase RNF31
Cysteine 551 of E3 ubiquitin-protein ligase RNF31
6sc6 A 717 A 744
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF31 between cysteines 717 and 744.
Details
Redox score ?
80
PDB code
6sc6
Structure name
dab3/hoip-rbr apo structure
Structure deposition date
2019-07-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
8
% buried
28
Peptide accession
Q96EP0
Residue number A
717
Residue number B
744
Peptide name
E3 ubiquitin-protein ligase RNF31
Ligandability
Cysteine 717 of E3 ubiquitin-protein ligase RNF31
Cysteine 744 of E3 ubiquitin-protein ligase RNF31
5edv A 825 A 828
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF31 between cysteines 825 and 828.
Details
Redox score ?
79
PDB code
5edv
Structure name
structure of the hoip-rbr/ubch5b~ubiquitin transfer complex
Structure deposition date
2015-10-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
7
% buried
42
Peptide accession
Q96EP0
Residue number A
825
Residue number B
828
Peptide name
E3 ubiquitin-protein ligase RNF31
Ligandability
Cysteine 825 of E3 ubiquitin-protein ligase RNF31
Cysteine 828 of E3 ubiquitin-protein ligase RNF31
4ljo A 874 A 893
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF31 between cysteines 874 and 893.
Details
Redox score ?
79
PDB code
4ljo
Structure name
structure of an active ligase (hoip)/ubiquitin transfer complex
Structure deposition date
2013-07-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
34
Minimum pKa ?
9
% buried
0
Peptide accession
Q96EP0
Residue number A
874
Residue number B
893
Peptide name
E3 ubiquitin-protein ligase RNF31
Ligandability
Cysteine 874 of E3 ubiquitin-protein ligase RNF31
Cysteine 893 of E3 ubiquitin-protein ligase RNF31
4ljp A 969 A 998
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF31 between cysteines 969 and 998.
Details
Redox score ?
78
PDB code
4ljp
Structure name
structure of an active ligase (hoip-h889a)/ubiquitin transfer complex
Structure deposition date
2013-07-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
6
% buried
52
Peptide accession
Q96EP0
Residue number A
969
Residue number B
998
Peptide name
E3 ubiquitin-protein ligase RNF31
Ligandability
Cysteine 969 of E3 ubiquitin-protein ligase RNF31
Cysteine 998 of E3 ubiquitin-protein ligase RNF31
6sc6 A 799 A 820
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF31 between cysteines 799 and 820.
Details
Redox score ?
78
PDB code
6sc6
Structure name
dab3/hoip-rbr apo structure
Structure deposition date
2019-07-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
73
Minimum pKa ?
5
% buried
nan
Peptide accession
Q96EP0
Residue number A
799
Residue number B
820
Peptide name
E3 ubiquitin-protein ligase RNF31
Ligandability
Cysteine 799 of E3 ubiquitin-protein ligase RNF31
Cysteine 820 of E3 ubiquitin-protein ligase RNF31
5edv A 719 A 744
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF31 between cysteines 719 and 744.
Details
Redox score ?
77
PDB code
5edv
Structure name
structure of the hoip-rbr/ubch5b~ubiquitin transfer complex
Structure deposition date
2015-10-22
Thiol separation (Å)
3
Half-sphere exposure sum ?
64
Minimum pKa ?
10
% buried
38
Peptide accession
Q96EP0
Residue number A
719
Residue number B
744
Peptide name
E3 ubiquitin-protein ligase RNF31
Ligandability
Cysteine 719 of E3 ubiquitin-protein ligase RNF31
Cysteine 744 of E3 ubiquitin-protein ligase RNF31
6sc9 A 702 A 725
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF31 between cysteines 702 and 725.
Details
Redox score ?
76
PDB code
6sc9
Structure name
dab3/hoip-rbr-hoipin-8
Structure deposition date
2019-07-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
44
Minimum pKa ?
9
% buried
0
Peptide accession
Q96EP0
Residue number A
702
Residue number B
725
Peptide name
E3 ubiquitin-protein ligase RNF31
Ligandability
Cysteine 702 of E3 ubiquitin-protein ligase RNF31
Cysteine 725 of E3 ubiquitin-protein ligase RNF31
6sc9 A 986 A 998
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF31 between cysteines 986 and 998.
Details
Redox score ?
76
PDB code
6sc9
Structure name
dab3/hoip-rbr-hoipin-8
Structure deposition date
2019-07-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
7
% buried
30
Peptide accession
Q96EP0
Residue number A
986
Residue number B
998
Peptide name
E3 ubiquitin-protein ligase RNF31
Ligandability
Cysteine 986 of E3 ubiquitin-protein ligase RNF31
Cysteine 998 of E3 ubiquitin-protein ligase RNF31
5edv A 744 A 747
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF31 between cysteines 744 and 747.
Details
Redox score ?
76
PDB code
5edv
Structure name
structure of the hoip-rbr/ubch5b~ubiquitin transfer complex
Structure deposition date
2015-10-22
Thiol separation (Å)
3
Half-sphere exposure sum ?
61
Minimum pKa ?
10
% buried
34
Peptide accession
Q96EP0
Residue number A
744
Residue number B
747
Peptide name
E3 ubiquitin-protein ligase RNF31
Ligandability
Cysteine 744 of E3 ubiquitin-protein ligase RNF31
Cysteine 747 of E3 ubiquitin-protein ligase RNF31
6sc5 A 702 A 722
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF31 between cysteines 702 and 722.
Details
Redox score ?
75
PDB code
6sc5
Structure name
dab3/hoip-rbr-ligand2
Structure deposition date
2019-07-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
8
% buried
6
Peptide accession
Q96EP0
Residue number A
702
Residue number B
722
Peptide name
E3 ubiquitin-protein ligase RNF31
Ligandability
Cysteine 702 of E3 ubiquitin-protein ligase RNF31
Cysteine 722 of E3 ubiquitin-protein ligase RNF31
5edv A 901 A 930
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF31 between cysteines 901 and 930.
Details
Redox score ?
75
PDB code
5edv
Structure name
structure of the hoip-rbr/ubch5b~ubiquitin transfer complex
Structure deposition date
2015-10-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
9
% buried
50
Peptide accession
Q96EP0
Residue number A
901
Residue number B
930
Peptide name
E3 ubiquitin-protein ligase RNF31
Ligandability
Cysteine 901 of E3 ubiquitin-protein ligase RNF31
Cysteine 930 of E3 ubiquitin-protein ligase RNF31
5edv B 898 B 930
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF31 between cysteines 898 and 930.
Details
Redox score ?
73
PDB code
5edv
Structure name
structure of the hoip-rbr/ubch5b~ubiquitin transfer complex
Structure deposition date
2015-10-22
Thiol separation (Å)
3
Half-sphere exposure sum ?
71
Minimum pKa ?
10
% buried
nan
Peptide accession
Q96EP0
Residue number A
898
Residue number B
930
Peptide name
E3 ubiquitin-protein ligase RNF31
Ligandability
Cysteine 898 of E3 ubiquitin-protein ligase RNF31
Cysteine 930 of E3 ubiquitin-protein ligase RNF31
If this tool was useful for finding a disulphide, please cite: