Ferrochelatase, mitochondrial
Intramolecular
Cysteine 406 and cysteine 411
Cysteine 323 and cysteine 360
Cysteine 196 and cysteine 403
Cysteine 403 and cysteine 406
Cysteine 196 and cysteine 406
Cysteine 403 and cysteine 411
Cysteine 196 and cysteine 411
Cysteine 196 and cysteine 197
4f4d A 406 A 411
A redox-regulated disulphide may form within Ferrochelatase, mitochondrial between cysteines 406 and 411.
Details
Redox score ?
82
PDB code
4f4d
Structure name
f337r variant of human ferrochelatase
Structure deposition date
2012-05-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
6
% buried
66
Peptide accession
P22830
Residue number A
406
Residue number B
411
Peptide name
Ferrochelatase, mitochondrial
Ligandability
Cysteine 406 of Ferrochelatase, mitochondrial
Cysteine 411 of Ferrochelatase, mitochondrial
2qd1 D 323 D 360
A redox-regulated disulphide may form within Ferrochelatase, mitochondrial between cysteines 323 and 360.
Details
Redox score ?
79
PDB code
2qd1
Structure name
2
Structure deposition date
2007-06-20
Thiol separation (Å)
3
Half-sphere exposure sum ?
60
Minimum pKa ?
9
% buried
38
Peptide accession
P22830
Residue number A
323
Residue number B
360
Peptide name
Ferrochelatase, mitochondrial
Ligandability
Cysteine 323 of Ferrochelatase, mitochondrial
Cysteine 360 of Ferrochelatase, mitochondrial
4klc A 196 A 403
A redox-regulated disulphide may form within Ferrochelatase, mitochondrial between cysteines 196 and 403.
Details
Redox score ?
72
PDB code
4klc
Structure name
e343d/f110a double mutant of human ferrochelatase
Structure deposition date
2013-05-07
Thiol separation (Å)
3
Half-sphere exposure sum ?
87
Minimum pKa ?
7
% buried
100
Peptide accession
P22830
Residue number A
196
Residue number B
403
Peptide name
Ferrochelatase, mitochondrial
Ligandability
Cysteine 196 of Ferrochelatase, mitochondrial
Cysteine 403 of Ferrochelatase, mitochondrial
3aqi B 903 B 906
A redox-regulated disulphide may form within Ferrochelatase, mitochondrial between cysteines 403 and 406 (903 and 906 respectively in this structure).
Details
Redox score ?
63
PDB code
3aqi
Structure name
h240a variant of human ferrochelatase
Structure deposition date
2010-11-03
Thiol separation (Å)
6
Half-sphere exposure sum ?
76
Minimum pKa ?
6
% buried
82
Peptide accession
P22830
Residue number A
403
Residue number B
406
Peptide name
Ferrochelatase, mitochondrial
Ligandability
Cysteine 403 of Ferrochelatase, mitochondrial
Cysteine 406 of Ferrochelatase, mitochondrial
4mk4 A 196 A 406
A redox-regulated disulphide may form within Ferrochelatase, mitochondrial between cysteines 196 and 406.
Details
Redox score ?
60
PDB code
4mk4
Structure name
s197c variant of human ferrochelatase
Structure deposition date
2013-09-04
Thiol separation (Å)
7
Half-sphere exposure sum ?
68
Minimum pKa ?
6
% buried
82
Peptide accession
P22830
Residue number A
196
Residue number B
406
Peptide name
Ferrochelatase, mitochondrial
Ligandability
Cysteine 196 of Ferrochelatase, mitochondrial
Cysteine 406 of Ferrochelatase, mitochondrial
7ct7 A 403 A 411
A redox-regulated disulphide may form within Ferrochelatase, mitochondrial between cysteines 403 and 411. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
53
PDB code
7ct7
Structure name
fech - inhibitor complex 2
Structure deposition date
2020-08-18
Thiol separation (Å)
7
Half-sphere exposure sum ?
81
Minimum pKa ?
7
% buried
88
Peptide accession
P22830
Residue number A
403
Residue number B
411
Peptide name
Ferrochelatase, mitochondrial
Ligandability
Cysteine 403 of Ferrochelatase, mitochondrial
Cysteine 411 of Ferrochelatase, mitochondrial
4mk4 A 196 A 411
A redox-regulated disulphide may form within Ferrochelatase, mitochondrial between cysteines 196 and 411. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
4mk4
Structure name
s197c variant of human ferrochelatase
Structure deposition date
2013-09-04
Thiol separation (Å)
6
Half-sphere exposure sum ?
73
Minimum pKa ?
16
% buried
88
Peptide accession
P22830
Residue number A
196
Residue number B
411
Peptide name
Ferrochelatase, mitochondrial
Ligandability
Cysteine 196 of Ferrochelatase, mitochondrial
Cysteine 411 of Ferrochelatase, mitochondrial
4mk4 A 196 A 197
A redox-regulated disulphide may form within Ferrochelatase, mitochondrial between cysteines 196 and 197. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
4mk4
Structure name
s197c variant of human ferrochelatase
Structure deposition date
2013-09-04
Thiol separation (Å)
7
Half-sphere exposure sum ?
74
Minimum pKa ?
12
% buried
100
Peptide accession
P22830
Residue number A
196
Residue number B
197
Peptide name
Ferrochelatase, mitochondrial
Ligandability
Cysteine 196 of Ferrochelatase, mitochondrial
Cysteine 197 of Ferrochelatase, mitochondrial
Cysteine 197 in protein B could not be asigned to a Uniprot residue.
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