ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Angiotensin-converting enzyme

Intramolecular
Cysteine 157 and cysteine 165
Cysteine 757 and cysteine 763
Cysteine 1143 and cysteine 1155
Cysteine 545 and cysteine 557
Cysteine 359 and cysteine 975
Cysteine 359 and cysteine 377
A redox-regulated disulphide may form within Angiotensin-converting enzyme between cysteines 157 and 165 (128 and 136 respectively in this structure).

Details

Redox score ?
87
PDB code
2c6n
Structure name
structure of human somatic angiontensin-i converting enzyme n domain with lisinopril
Structure deposition date
2005-11-10
Thiol separation (Å)
2
Half-sphere exposure sum ?
46
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q59GY8
Residue number A
157
Residue number B
165
Peptide name
Angiotensin-converting enzyme

Ligandability

Cysteine 157 of Angiotensin-converting enzyme

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 165 of Angiotensin-converting enzyme

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 Angiotensin-converting enzyme between cysteines 757 and 763 (152 and 158 respectively in this structure).

Details

Redox score ?
85
PDB code
1o86
Structure name
crystal structure of human angiotensin converting enzyme in complex with lisinopril
Structure deposition date
2002-11-25
Thiol separation (Å)
2
Half-sphere exposure sum ?
41
Minimum pKa ?
nan
% buried
nan
Peptide accession
P22966
Residue number A
757
Residue number B
763
Peptide name
Angiotensin-converting enzyme

Ligandability

Cysteine 757 of Angiotensin-converting enzyme

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 763 of Angiotensin-converting enzyme

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 Angiotensin-converting enzyme between cysteines 1143 and 1155 (538 and 550 respectively in this structure).

Details

Redox score ?
82
PDB code
1o8a
Structure name
crystal structure of human angiotensin converting enzyme (native)
Structure deposition date
2002-11-26
Thiol separation (Å)
2
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P22966
Residue number A
1143
Residue number B
1155
Peptide name
Angiotensin-converting enzyme

Ligandability

Cysteine 1143 of Angiotensin-converting enzyme

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 1155 of Angiotensin-converting enzyme

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 Angiotensin-converting enzyme between cysteines 545 and 557 (516 and 528 respectively in this structure).

Details

Redox score ?
82
PDB code
2c6n
Structure name
structure of human somatic angiontensin-i converting enzyme n domain with lisinopril
Structure deposition date
2005-11-10
Thiol separation (Å)
2
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q59GY8
Residue number A
545
Residue number B
557
Peptide name
Angiotensin-converting enzyme

Ligandability

Cysteine 545 of Angiotensin-converting enzyme

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 557 of Angiotensin-converting enzyme

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 Angiotensin-converting enzyme between cysteines 359 and 975 (352 and 370 respectively in this structure).

Details

Redox score ?
80
PDB code
1o86
Structure name
crystal structure of human angiotensin converting enzyme in complex with lisinopril
Structure deposition date
2002-11-25
Thiol separation (Å)
2
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
P22966
Residue number A
359
Residue number B
975
Peptide name
Angiotensin-converting enzyme

Ligandability

Cysteine 359 of Angiotensin-converting enzyme

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 975 of Angiotensin-converting enzyme

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 Angiotensin-converting enzyme between cysteines 359 and 377 (330 and 348 respectively in this structure).

Details

Redox score ?
80
PDB code
5am9
Structure name
crystal structure of the angiotensin-1 converting enzyme n-domain in complex with amyloid-beta 10-16
Structure deposition date
2015-03-10
Thiol separation (Å)
2
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
P12821
Residue number A
359
Residue number B
377
Peptide name
Angiotensin-converting enzyme

Ligandability

Cysteine 359 of Angiotensin-converting enzyme

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 377 of Angiotensin-converting enzyme

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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