ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

Cholinesterase

Intramolecular
Cysteine 280 and cysteine 291
Cysteine 428 and cysteine 547
Cysteine 93 and cysteine 120
Cysteine 93 and cysteine 94
Cysteine 94 and cysteine 120
A redox-regulated disulphide may form within Cholinesterase between cysteines 280 and 291 (252 and 263 respectively in this structure).

Details

Redox score ?
82
PDB code
6ez2
Structure name
human butyrylcholinesterase carbamylated
Structure deposition date
2017-11-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P06276
Residue number A
280
Residue number B
291
Peptide name
Cholinesterase

Ligandability

Cysteine 280 of Cholinesterase

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 291 of Cholinesterase

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 Cholinesterase between cysteines 428 and 547 (400 and 519 respectively in this structure).

Details

Redox score ?
81
PDB code
6eqp
Structure name
human butyrylcholinesterase in complex with ethopropazine
Structure deposition date
2017-10-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P06276
Residue number A
428
Residue number B
547
Peptide name
Cholinesterase

Ligandability

Cysteine 428 of Cholinesterase

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 547 of Cholinesterase

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 Cholinesterase between cysteines 93 and 120 (65 and 92 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
6emi
Structure name
crystal structure of a variant of human butyrylcholinesterase expressed in bacteria
Structure deposition date
2017-10-02
Thiol separation (Å)
5
Half-sphere exposure sum ?
83
Minimum pKa ?
11
% buried
100
Peptide accession
P06276
Residue number A
93
Residue number B
120
Peptide name
Cholinesterase

Ligandability

Cysteine 93 of Cholinesterase

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 120 of Cholinesterase

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 Cholinesterase between cysteines 93 and 94 (65 and 66 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
6esj
Structure name
human butyrylcholinesterase in complex with propidium
Structure deposition date
2017-10-20
Thiol separation (Å)
5
Half-sphere exposure sum ?
79
Minimum pKa ?
13
% buried
nan
Peptide accession
P06276
Residue number A
93
Residue number B
94
Peptide name
Cholinesterase

Ligandability

Cysteine 93 of Cholinesterase

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 94 of Cholinesterase

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 Cholinesterase between cysteines 94 and 120 (66 and 92 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
7aiy
Structure name
crystal structure of human butyrylcholinesterase in complex with 2-{1- [4-(12-amino-3-chloro-6,7,10,11-tetrahydro-7,11- methanocycloocta[b]quinolin-9-yl)butyl]-1h-1,2,3-triazol-4-yl}-n-[4- hydroxy-3-methoxybenzyl]acetamide
Structure deposition date
2020-09-28
Thiol separation (Å)
7
Half-sphere exposure sum ?
78
Minimum pKa ?
11
% buried
nan
Peptide accession
P06276
Residue number A
94
Residue number B
120
Peptide name
Cholinesterase

Ligandability

Cysteine 94 of Cholinesterase

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 120 of Cholinesterase

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.

If this tool was useful for finding a disulphide, please cite: