ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Ferrochelatase

Intramolecular
Cysteine 399 and cysteine 404
Cysteine 316 and cysteine 353
Cysteine 189 and cysteine 396
Cysteine 396 and cysteine 399
Cysteine 189 and cysteine 399
Cysteine 396 and cysteine 404
Cysteine 189 and cysteine 404
A redox-regulated disulphide may form within Ferrochelatase between cysteines 399 and 404 (406 and 411 respectively in this structure).

Details

Redox score ?
80
PDB code
2qd2
Structure name
f110a variant of human ferrochelatase with protoheme bound
Structure deposition date
2007-06-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
6
% buried
76
Peptide accession
Q7KZA3
Residue number A
399
Residue number B
404
Peptide name
Ferrochelatase

Ligandability

Cysteine 399 of Ferrochelatase

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 404 of Ferrochelatase

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 Ferrochelatase between cysteines 316 and 353 (323 and 360 respectively in this structure).

Details

Redox score ?
73
PDB code
2qd2
Structure name
f110a variant of human ferrochelatase with protoheme bound
Structure deposition date
2007-06-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
10
% buried
32
Peptide accession
Q7KZA3
Residue number A
316
Residue number B
353
Peptide name
Ferrochelatase

Ligandability

Cysteine 316 of Ferrochelatase

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 353 of Ferrochelatase

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 Ferrochelatase between cysteines 189 and 396 (196 and 403 respectively in this structure).

Details

Redox score ?
70
PDB code
2qd2
Structure name
f110a variant of human ferrochelatase with protoheme bound
Structure deposition date
2007-06-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
88
Minimum pKa ?
7
% buried
100
Peptide accession
Q7KZA3
Residue number A
189
Residue number B
396
Peptide name
Ferrochelatase

Ligandability

Cysteine 189 of Ferrochelatase

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 396 of Ferrochelatase

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 Ferrochelatase between cysteines 396 and 399 (403 and 406 respectively in this structure).

Details

Redox score ?
64
PDB code
2qd2
Structure name
f110a variant of human ferrochelatase with protoheme bound
Structure deposition date
2007-06-20
Thiol separation (Å)
6
Half-sphere exposure sum ?
78
Minimum pKa ?
6
% buried
84
Peptide accession
Q7KZA3
Residue number A
396
Residue number B
399
Peptide name
Ferrochelatase

Ligandability

Cysteine 396 of Ferrochelatase

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 399 of Ferrochelatase

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 Ferrochelatase between cysteines 189 and 399 (196 and 406 respectively in this structure).

Details

Redox score ?
61
PDB code
2qd2
Structure name
f110a variant of human ferrochelatase with protoheme bound
Structure deposition date
2007-06-20
Thiol separation (Å)
7
Half-sphere exposure sum ?
76
Minimum pKa ?
6
% buried
84
Peptide accession
Q7KZA3
Residue number A
189
Residue number B
399
Peptide name
Ferrochelatase

Ligandability

Cysteine 189 of Ferrochelatase

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 399 of Ferrochelatase

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 Ferrochelatase between cysteines 396 and 404 (403 and 411 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
2qd2
Structure name
f110a variant of human ferrochelatase with protoheme bound
Structure deposition date
2007-06-20
Thiol separation (Å)
7
Half-sphere exposure sum ?
82
Minimum pKa ?
8
% buried
91
Peptide accession
Q7KZA3
Residue number A
396
Residue number B
404
Peptide name
Ferrochelatase

Ligandability

Cysteine 396 of Ferrochelatase

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 404 of Ferrochelatase

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 Ferrochelatase between cysteines 189 and 404 (196 and 411 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
2qd2
Structure name
f110a variant of human ferrochelatase with protoheme bound
Structure deposition date
2007-06-20
Thiol separation (Å)
5
Half-sphere exposure sum ?
77
Minimum pKa ?
16
% buried
91
Peptide accession
Q7KZA3
Residue number A
189
Residue number B
404
Peptide name
Ferrochelatase

Ligandability

Cysteine 189 of Ferrochelatase

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 404 of Ferrochelatase

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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