Ketohexokinase
Intermolecular
Cysteine 98 and cysteine 98
Cysteine 32 and cysteine 98
Cysteine 98 and cysteine 99
Intramolecular
Cysteine 8 and cysteine 47
Cysteine 8 and cysteine 57
Cysteine 47 and cysteine 57
Cysteine 47 and cysteine 47
Cysteine 282 and cysteine 289
3b3l A 98 B 98
A redox-regulated disulphide may form between two units of Ketohexokinase at cysteines 98 and 98.
Details
Redox score ?
67
PDB code
3b3l
Structure name
crystal structures of alternatively-spliced isoforms of human ketohexokinase
Structure deposition date
2007-10-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
88
Minimum pKa ?
8
% buried
100
Peptide A name
Ketohexokinase
Peptide B name
Ketohexokinase
Peptide A accession
P50053
Peptide B accession
P50053
Peptide A residue number
98
Peptide B residue number
98
Ligandability
5wbr A 32 B 98
A redox-regulated disulphide may form between two units of Ketohexokinase at cysteines 32 and 98. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
36
PDB code
5wbr
Structure name
structure of human ketohexokinase complexed with hits from fragment screening
Structure deposition date
2017-06-29
Thiol separation (Å)
9
Half-sphere exposure sum ?
74
Minimum pKa ?
12
% buried
82
Peptide A name
Ketohexokinase
Peptide B name
Ketohexokinase
Peptide A accession
P50053
Peptide B accession
P50053
Peptide A residue number
32
Peptide B residue number
98
Ligandability
Cysteine 32 of Ketohexokinase
Cysteine 98 of Ketohexokinase
6w0y A 98 B 99
A redox-regulated disulphide may form between two units of Ketohexokinase at cysteines 98 and 99. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
27
PDB code
6w0y
Structure name
structure of khk in complex with compound 6 (2-[(1~{r},5~{s})-3-[5- cyano-6-[(2~{s},3~{r})-2-methyl-3-oxidanyl-azetidin-1-yl]-4- (trifluoromethyl)pyridin-2-yl]-3-azabicyclo[3
Structure deposition date
2020-03-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
90
Minimum pKa ?
12
% buried
88
Peptide A name
Ketohexokinase
Peptide B name
Ketohexokinase
Peptide A accession
P50053
Peptide B accession
P50053
Peptide A residue number
98
Peptide B residue number
99
Ligandability
Cysteine 98 of Ketohexokinase
Cysteine 99 of Ketohexokinase
3b3l C 8 C 47
A redox-regulated disulphide may form within Ketohexokinase between cysteines 8 and 47.
Details
Redox score ?
66
PDB code
3b3l
Structure name
crystal structures of alternatively-spliced isoforms of human ketohexokinase
Structure deposition date
2007-10-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
97
Minimum pKa ?
10
% buried
100
Peptide accession
P50053
Residue number A
8
Residue number B
47
Peptide name
Ketohexokinase
Ligandability
Cysteine 8 of Ketohexokinase
Cysteine 47 of Ketohexokinase
3nbv A 8 A 57
A redox-regulated disulphide may form within Isoform A of Ketohexokinase between cysteines 8 and 57. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
55
PDB code
3nbv
Structure name
x-ray structure of ketohexokinase in complex with amp-pnp and fructose
Structure deposition date
2010-06-04
Thiol separation (Å)
6
Half-sphere exposure sum ?
90
Minimum pKa ?
10
% buried
94
Peptide accession
P50053-2
Residue number A
8
Residue number B
57
Peptide name
Isoform A of Ketohexokinase
Ligandability
Cysteine 8 of Isoform A of Ketohexokinase
Cysteine 57 of Isoform A of Ketohexokinase
6ul7 A 47 A 57
A redox-regulated disulphide may form within Ketohexokinase between cysteines 47 and 57. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
53
PDB code
6ul7
Structure name
structure of human ketohexokinase-c in complex with fructose, no3, and osthole
Structure deposition date
2019-10-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
94
Minimum pKa ?
14
% buried
96
Peptide accession
P50053
Residue number A
47
Residue number B
57
Peptide name
Ketohexokinase
Ligandability
Cysteine 47 of Ketohexokinase
Cysteine 57 of Ketohexokinase
3qai A 98 A 99
A redox-regulated disulphide may form within Isoform A of Ketohexokinase between cysteines 47 and 47 (98 and 99 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
33
PDB code
3qai
Structure name
x-ray structure of ketohexokinase in complex with a pyrimidopyrimidine analog 3
Structure deposition date
2011-01-11
Thiol separation (Å)
7
Half-sphere exposure sum ?
94
Minimum pKa ?
15
% buried
100
Peptide accession
P50053-2
Residue number A
47
Residue number B
47
Peptide name
Isoform A of Ketohexokinase
Ligandability
Cysteine 47 of Isoform A of Ketohexokinase
Cysteine 47 of Isoform A of Ketohexokinase
Uncertain whether structure cysteine 98 has been assigned to correct residue.
Uncertain whether structure cysteine 99 has been assigned to correct residue.
3nbv B 282 B 289
A redox-regulated disulphide may form within Isoform A of Ketohexokinase between cysteines 282 and 289. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
32
PDB code
3nbv
Structure name
x-ray structure of ketohexokinase in complex with amp-pnp and fructose
Structure deposition date
2010-06-04
Thiol separation (Å)
10
Half-sphere exposure sum ?
75
Minimum pKa ?
10
% buried
65
Peptide accession
P50053-2
Residue number A
282
Residue number B
289
Peptide name
Isoform A of Ketohexokinase
Ligandability
Cysteine 282 of Isoform A of Ketohexokinase
Cysteine 289 of Isoform A of Ketohexokinase
If this tool was useful for finding a disulphide, please cite: