Elongin-C
Intermolecular
Cysteine 193 of Suppressor of cytokine signaling 3 and cysteine 112
Cysteine 112 and cysteine 162 of von Hippel-Lindau disease tumor suppressor
Cysteine 112 and cysteine 178 of Suppressor of cytokine signaling
Cysteine 262 of Ankyrin repeat and SOCS box protein 9 and cysteine 112
Cysteine 112 and cysteine 167 of Suppressor of cytokine signaling 2
Cysteine 393 of Suppressor of cytokine signaling 4 and cysteine 112
Intramolecular
Cysteine 74 and cysteine 112 L
2jz3 A 8 C 112
A redox-regulated disulphide may form between cysteine 193 of Suppressor of cytokine signaling 3 and cysteine 112 of Elongin-C (8 and 112 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
53
PDB code
2jz3
Structure name
socs box elonginbc ternary complex
Structure deposition date
2007-12-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
nan
Minimum pKa ?
10
% buried
24
Peptide A name
Suppressor of cytokine signaling 3
Peptide B name
Elongin-C
Peptide A accession
O35718
Peptide B accession
P83940
Peptide A residue number
193
Peptide B residue number
112
Ligandability
Cysteine 193 of Suppressor of cytokine signaling 3
Cysteine 112 of Elongin-C
6i7q C 112 V 162
A redox-regulated disulphide may form between cysteine 112 of Elongin-C and cysteine 162 of von Hippel-Lindau disease tumor suppressor. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
6i7q
Structure name
structure of pvhl-elongin b-elongin c (vcb) in complex with hydroxylated-hif-2alpha (523-542) in the c2221 form
Structure deposition date
2018-11-17
Thiol separation (Å)
8
Half-sphere exposure sum ?
nan
Minimum pKa ?
13
% buried
96
Peptide A name
Elongin-C
Peptide B name
von Hippel-Lindau disease tumor suppressor
Peptide A accession
Q2KII4
Peptide B accession
P40337
Peptide A residue number
112
Peptide B residue number
162
Ligandability
Cysteine 112 of Elongin-C
Cysteine 162 of von Hippel-Lindau disease tumor suppressor
6c5x C 112 A 178
A redox-regulated disulphide may form between cysteine 112 of Elongin-C and cysteine 178 of Suppressor of cytokine signaling. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
6c5x
Structure name
crystal structure of socs1 in complex with elonginb and elonginc
Structure deposition date
2018-01-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
nan
Minimum pKa ?
12
% buried
92
Peptide A name
Elongin-C
Peptide B name
Suppressor of cytokine signaling
Peptide A accession
Q15369
Peptide B accession
C0LEJ4
Peptide A residue number
112
Peptide B residue number
178
Ligandability
Cysteine 112 of Elongin-C
Cysteine 178 of Suppressor of cytokine signaling
3zkj A 262 B 112
A redox-regulated disulphide may form between cysteine 262 of Ankyrin repeat and SOCS box protein 9 and cysteine 112 of Elongin-C. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
3zkj
Structure name
crystal structure of ankyrin repeat and socs box-containing protein 9 (asb9) in complex with elonginb and elonginc
Structure deposition date
2013-01-23
Thiol separation (Å)
9
Half-sphere exposure sum ?
nan
Minimum pKa ?
13
% buried
88
Peptide A name
Ankyrin repeat and SOCS box protein 9
Peptide B name
Elongin-C
Peptide A accession
Q96DX5
Peptide B accession
Q15369
Peptide A residue number
262
Peptide B residue number
112
Ligandability
Cysteine 262 of Ankyrin repeat and SOCS box protein 9
Cysteine 112 of Elongin-C
6i4x C 112 A 167
A redox-regulated disulphide may form between cysteine 112 of Elongin-C and cysteine 167 of Suppressor of cytokine signaling 2. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
6i4x
Structure name
crystal structure of socs2:elongin c:elongin b in complex with erythropoietin receptor peptide
Structure deposition date
2018-11-12
Thiol separation (Å)
9
Half-sphere exposure sum ?
nan
Minimum pKa ?
13
% buried
96
Peptide A name
Elongin-C
Peptide B name
Suppressor of cytokine signaling 2
Peptide A accession
Q15369
Peptide B accession
O14508
Peptide A residue number
112
Peptide B residue number
167
Ligandability
Cysteine 112 of Elongin-C
Cysteine 167 of Suppressor of cytokine signaling 2
2izv A 393 C 112
A redox-regulated disulphide may form between cysteine 393 of Suppressor of cytokine signaling 4 and cysteine 112 of Elongin-C. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
2izv
Structure name
crystal structure of socs-4 in complex with elongin-b and elongin-c at 2
Structure deposition date
2006-07-26
Thiol separation (Å)
9
Half-sphere exposure sum ?
nan
Minimum pKa ?
13
% buried
94
Peptide A name
Suppressor of cytokine signaling 4
Peptide B name
Elongin-C
Peptide A accession
Q8WXH5
Peptide B accession
Q15369
Peptide A residue number
393
Peptide B residue number
112
Ligandability
Cysteine 393 of Suppressor of cytokine signaling 4
Cysteine 112 of Elongin-C
6gfz H 74 H 112
A redox-regulated disulphide may form within Elongin-C between cysteines 74 and 112. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
36
PDB code
6gfz
Structure name
pvhl:elob:eloc in complex with modified vh032 containing (3s,4s)-3- fluoro-4-hydroxyproline (ligand 14b)
Structure deposition date
2018-05-02
Thiol separation (Å)
9
Half-sphere exposure sum ?
nan
Minimum pKa ?
13
% buried
100
Peptide accession
Q15369
Residue number A
74
Residue number B
112
Peptide name
Elongin-C
Ligandability
Cysteine 74 of Elongin-C
Cysteine 112 of Elongin-C
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