ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Chitotriosidase-1

Intermolecular
Cysteine 462 and cysteine 420
Cysteine 440 and cysteine 462
Intramolecular
Cysteine 420 and cysteine 440
Cysteine 307 and cysteine 370
Cysteine 450 and cysteine 463
Cysteine 460 and cysteine 462
Cysteine 26 and cysteine 51
Cysteine 462 and cysteine 463
Cysteine 460 and cysteine 463
Cysteine 450 and cysteine 462
Cysteine 450 and cysteine 460
A redox-regulated disulphide may form between two units of Chitotriosidase-1 at cysteines 462 and 420. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
5hbf
Structure name
crystal structure of human full-length chitotriosidase (chit1)
Structure deposition date
2015-12-31
Thiol separation (Å)
10
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide A name
Chitotriosidase-1
Peptide B name
Chitotriosidase-1
Peptide A accession
Q13231
Peptide B accession
Q13231
Peptide A residue number
462
Peptide B residue number
420

Ligandability

Cysteine 462 of Chitotriosidase-1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 420 of Chitotriosidase-1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form between two units of Chitotriosidase-1 at cysteines 440 and 462. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
5hbf
Structure name
crystal structure of human full-length chitotriosidase (chit1)
Structure deposition date
2015-12-31
Thiol separation (Å)
9
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide A name
Chitotriosidase-1
Peptide B name
Chitotriosidase-1
Peptide A accession
Q13231
Peptide B accession
Q13231
Peptide A residue number
440
Peptide B residue number
462

Ligandability

Cysteine 440 of Chitotriosidase-1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 462 of Chitotriosidase-1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Chitotriosidase-1 between cysteines 420 and 440.

Details

Redox score ?
87
PDB code
5hbf
Structure name
crystal structure of human full-length chitotriosidase (chit1)
Structure deposition date
2015-12-31
Thiol separation (Å)
2
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q13231
Residue number A
420
Residue number B
440
Peptide name
Chitotriosidase-1

Ligandability

Cysteine 420 of Chitotriosidase-1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 440 of Chitotriosidase-1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Chitotriosidase-1 between cysteines 307 and 370 (307 and 372 respectively in this structure).

Details

Redox score ?
85
PDB code
1wb0
Structure name
specificity and affinity of natural product cyclopentapeptide inhibitor argifin against human chitinase
Structure deposition date
2004-10-29
Thiol separation (Å)
2
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q13231
Residue number A
307
Residue number B
370
Peptide name
Chitotriosidase-1

Ligandability

Cysteine 307 of Chitotriosidase-1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 370 of Chitotriosidase-1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Chitotriosidase-1 between cysteines 450 and 463.

Details

Redox score ?
81
PDB code
5hbf
Structure name
crystal structure of human full-length chitotriosidase (chit1)
Structure deposition date
2015-12-31
Thiol separation (Å)
2
Half-sphere exposure sum ?
85
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q13231
Residue number A
450
Residue number B
463
Peptide name
Chitotriosidase-1

Ligandability

Cysteine 450 of Chitotriosidase-1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 463 of Chitotriosidase-1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Chitotriosidase-1 between cysteines 460 and 462.

Details

Redox score ?
81
PDB code
5hbf
Structure name
crystal structure of human full-length chitotriosidase (chit1)
Structure deposition date
2015-12-31
Thiol separation (Å)
2
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q13231
Residue number A
460
Residue number B
462
Peptide name
Chitotriosidase-1

Ligandability

Cysteine 460 of Chitotriosidase-1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 462 of Chitotriosidase-1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Chitotriosidase-1 between cysteines 26 and 51.

Details

Redox score ?
79
PDB code
6jjr
Structure name
crystal structure of human chitotriosidase-1 (hchit1) catalytic domain in complex with compound 2-8-14
Structure deposition date
2019-02-26
Thiol separation (Å)
2
Half-sphere exposure sum ?
88
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q13231
Residue number A
26
Residue number B
51
Peptide name
Chitotriosidase-1

Ligandability

Cysteine 26 of Chitotriosidase-1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 51 of Chitotriosidase-1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Chitotriosidase-1 between cysteines 462 and 463. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
5hbf
Structure name
crystal structure of human full-length chitotriosidase (chit1)
Structure deposition date
2015-12-31
Thiol separation (Å)
7
Half-sphere exposure sum ?
84
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q13231
Residue number A
462
Residue number B
463
Peptide name
Chitotriosidase-1

Ligandability

Cysteine 462 of Chitotriosidase-1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 463 of Chitotriosidase-1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Chitotriosidase-1 between cysteines 460 and 463. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
5hbf
Structure name
crystal structure of human full-length chitotriosidase (chit1)
Structure deposition date
2015-12-31
Thiol separation (Å)
8
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q13231
Residue number A
460
Residue number B
463
Peptide name
Chitotriosidase-1

Ligandability

Cysteine 460 of Chitotriosidase-1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 463 of Chitotriosidase-1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Chitotriosidase-1 between cysteines 450 and 462. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
5hbf
Structure name
crystal structure of human full-length chitotriosidase (chit1)
Structure deposition date
2015-12-31
Thiol separation (Å)
8
Half-sphere exposure sum ?
85
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q13231
Residue number A
450
Residue number B
462
Peptide name
Chitotriosidase-1

Ligandability

Cysteine 450 of Chitotriosidase-1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 462 of Chitotriosidase-1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Chitotriosidase-1 between cysteines 450 and 460. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
5hbf
Structure name
crystal structure of human full-length chitotriosidase (chit1)
Structure deposition date
2015-12-31
Thiol separation (Å)
9
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q13231
Residue number A
450
Residue number B
460
Peptide name
Chitotriosidase-1

Ligandability

Cysteine 450 of Chitotriosidase-1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 460 of Chitotriosidase-1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

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