Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial
Intermolecular
Cysteine 236 and cysteine 254 of Isocitrate dehydrogenase [NAD] subunit beta, mitochondrial
Cysteine 222 and cysteine 222
Cysteine 263 and cysteine 254 of Isoform A of Isocitrate dehydrogenase [NAD] subunit beta, mitochondrial
Intramolecular
Cysteine 127 and cysteine 263
Cysteine 351 and cysteine 359
Cysteine 236 and cysteine 263
6kde A 209 B 220
A redox-regulated disulphide may form between cysteine 236 of Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial and cysteine 254 of Isocitrate dehydrogenase [NAD] subunit beta, mitochondrial (209 and 220 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
6kde
Structure name
crystal structure of the alpha beta heterodimer of human idh3 in complex with ca(2+)
Structure deposition date
2019-07-02
Thiol separation (Å)
6
Half-sphere exposure sum ?
91
Minimum pKa ?
13
% buried
100
Peptide A name
Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial
Peptide B name
Isocitrate dehydrogenase [NAD] subunit beta, mitochondrial
Peptide A accession
P50213
Peptide B accession
O43837
Peptide A residue number
236
Peptide B residue number
254
Ligandability
Cysteine 236 of Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial
Cysteine 254 of Isocitrate dehydrogenase [NAD] subunit beta, mitochondrial
6kdf A 195 K 195
A redox-regulated disulphide may form between two units of Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial at cysteines 222 and 222 (195 and 195 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
6kdf
Structure name
crystal structure of the alpha beta heterodimer of human idh3 in apo form
Structure deposition date
2019-07-02
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
10
% buried
64
Peptide A name
Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial
Peptide B name
Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial
Peptide A accession
P50213
Peptide B accession
P50213
Peptide A residue number
222
Peptide B residue number
222
Ligandability
8grb I 236 J 220
A redox-regulated disulphide may form between cysteine 263 of Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial and cysteine 254 of Isoform A of Isocitrate dehydrogenase [NAD] subunit beta, mitochondrial (236 and 220 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
19
PDB code
8grb
Structure name
crystal structure of a constitutively active mutant of the alpha beta heterodimer of human idh3
Structure deposition date
2022-09-01
Thiol separation (Å)
10
Half-sphere exposure sum ?
94
Minimum pKa ?
14
% buried
100
Peptide A name
Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial
Peptide B name
Isoform A of Isocitrate dehydrogenase [NAD] subunit beta, mitochondrial
Peptide A accession
P50213
Peptide B accession
O43837-2
Peptide A residue number
263
Peptide B residue number
254
Ligandability
Cysteine 263 of Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial
Cysteine 254 of Isoform A of Isocitrate dehydrogenase [NAD] subunit beta, mitochondrial
7ce3 C 100 C 236
A redox-regulated disulphide may form within Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial between cysteines 127 and 263 (100 and 236 respectively in this structure).
Details
Redox score ?
64
PDB code
7ce3
Structure name
crystal structure of human idh3 holoenzyme in apo form
Structure deposition date
2020-06-21
Thiol separation (Å)
5
Half-sphere exposure sum ?
90
Minimum pKa ?
8
% buried
100
Peptide accession
P50213
Residue number A
127
Residue number B
263
Peptide name
Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial
Ligandability
Cysteine 127 of Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial
Cysteine 263 of Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial
8gs5 O 324 O 332
A redox-regulated disulphide may form within Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial between cysteines 351 and 359 (324 and 332 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
8gs5
Structure name
crystal structure of a constitutively active mutant of human idh3 holoenzyme in apo form
Structure deposition date
2022-09-04
Thiol separation (Å)
10
Half-sphere exposure sum ?
63
Minimum pKa ?
10
% buried
50
Peptide accession
P50213
Residue number A
351
Residue number B
359
Peptide name
Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial
Ligandability
Cysteine 351 of Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial
Cysteine 359 of Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial
6kdf K 209 K 236
A redox-regulated disulphide may form within Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial between cysteines 236 and 263 (209 and 236 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
28
PDB code
6kdf
Structure name
crystal structure of the alpha beta heterodimer of human idh3 in apo form
Structure deposition date
2019-07-02
Thiol separation (Å)
9
Half-sphere exposure sum ?
98
Minimum pKa ?
12
% buried
100
Peptide accession
P50213
Residue number A
236
Residue number B
263
Peptide name
Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial
Ligandability
Cysteine 236 of Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial
Cysteine 263 of Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial
If this tool was useful for finding a disulphide, please cite: