Hepcidin
Intermolecular
Cysteine 73 and cysteine 96 of Neutrophil gelatinase-associated lipocalin
Cysteine 81 and cysteine 96 of Neutrophil gelatinase-associated lipocalin
Cysteine 73 and cysteine 195 of Neutrophil gelatinase-associated lipocalin
Cysteine 81 and cysteine 195 of Neutrophil gelatinase-associated lipocalin
Cysteine 82 and cysteine 326 of Solute carrier family 40 member 1
Cysteine 66 and cysteine 326 of Solute carrier family 40 member 1
Cysteine 82 and cysteine 96 of Neutrophil gelatinase-associated lipocalin
Cysteine 69 and cysteine 96 of Neutrophil gelatinase-associated lipocalin
Cysteine 72 and cysteine 96 of Neutrophil gelatinase-associated lipocalin
Intramolecular
Cysteine 70 and cysteine 78
More...Cysteine 66 and cysteine 82
Cysteine 72 and cysteine 73
Cysteine 72 and cysteine 81
Cysteine 69 and cysteine 81
Cysteine 69 and cysteine 73
Cysteine 81 and cysteine 82
Cysteine 73 and cysteine 82
Cysteine 69 and cysteine 70
Cysteine 66 and cysteine 72
Cysteine 69 and cysteine 72
Cysteine 69 and cysteine 78
Cysteine 69 and cysteine 82
Cysteine 66 and cysteine 81
Cysteine 70 and cysteine 73
Cysteine 72 and cysteine 82
Cysteine 70 and cysteine 81
Cysteine 78 and cysteine 81
Cysteine 70 and cysteine 72
Cysteine 73 and cysteine 81
Cysteine 73 and cysteine 78
Cysteine 66 and cysteine 73
Cysteine 66 and cysteine 69
Cysteine 72 and cysteine 78
4qae R 14 A 76
A redox-regulated disulphide may form between cysteine 73 of Hepcidin and cysteine 96 of Neutrophil gelatinase-associated lipocalin (14 and 76 respectively in this structure).
Details
Redox score ?
75
PDB code
4qae
Structure name
crystal structure of an engineered lipocalin (anticalin) in complex with human hepcidin
Structure deposition date
2014-05-04
Thiol separation (Å)
3
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide A name
Hepcidin
Peptide B name
Neutrophil gelatinase-associated lipocalin
Peptide A accession
P81172
Peptide B accession
P80188
Peptide A residue number
73
Peptide B residue number
96
Ligandability
Cysteine 73 of Hepcidin
Cysteine 96 of Neutrophil gelatinase-associated lipocalin
4qae S 22 F 76
A redox-regulated disulphide may form between cysteine 81 of Hepcidin and cysteine 96 of Neutrophil gelatinase-associated lipocalin (22 and 76 respectively in this structure).
Details
Redox score ?
66
PDB code
4qae
Structure name
crystal structure of an engineered lipocalin (anticalin) in complex with human hepcidin
Structure deposition date
2014-05-04
Thiol separation (Å)
5
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide A name
Hepcidin
Peptide B name
Neutrophil gelatinase-associated lipocalin
Peptide A accession
P81172
Peptide B accession
P80188
Peptide A residue number
81
Peptide B residue number
96
Ligandability
Cysteine 81 of Hepcidin
Cysteine 96 of Neutrophil gelatinase-associated lipocalin
4qae P 14 B 175
A redox-regulated disulphide may form between cysteine 73 of Hepcidin and cysteine 195 of Neutrophil gelatinase-associated lipocalin (14 and 175 respectively in this structure).
Details
Redox score ?
63
PDB code
4qae
Structure name
crystal structure of an engineered lipocalin (anticalin) in complex with human hepcidin
Structure deposition date
2014-05-04
Thiol separation (Å)
5
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide A name
Hepcidin
Peptide B name
Neutrophil gelatinase-associated lipocalin
Peptide A accession
P81172
Peptide B accession
P80188
Peptide A residue number
73
Peptide B residue number
195
Ligandability
Cysteine 73 of Hepcidin
Cysteine 195 of Neutrophil gelatinase-associated lipocalin
4qae S 22 F 175
A redox-regulated disulphide may form between cysteine 81 of Hepcidin and cysteine 195 of Neutrophil gelatinase-associated lipocalin (22 and 175 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
54
PDB code
4qae
Structure name
crystal structure of an engineered lipocalin (anticalin) in complex with human hepcidin
Structure deposition date
2014-05-04
Thiol separation (Å)
7
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide A name
Hepcidin
Peptide B name
Neutrophil gelatinase-associated lipocalin
Peptide A accession
P81172
Peptide B accession
P80188
Peptide A residue number
81
Peptide B residue number
195
Ligandability
Cysteine 81 of Hepcidin
Cysteine 195 of Neutrophil gelatinase-associated lipocalin
6wbv B 23 A 326
A redox-regulated disulphide may form between cysteine 82 of Hepcidin and cysteine 326 of Solute carrier family 40 member 1 (23 and 326 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
52
PDB code
6wbv
Structure name
structure of human ferroportin bound to hepcidin and cobalt in lipid nanodisc
Structure deposition date
2020-03-27
Thiol separation (Å)
7
Half-sphere exposure sum ?
75
Minimum pKa ?
9
% buried
nan
Peptide A name
Hepcidin
Peptide B name
Solute carrier family 40 member 1
Peptide A accession
P81172
Peptide B accession
Q9NP59
Peptide A residue number
82
Peptide B residue number
326
Ligandability
Cysteine 82 of Hepcidin
Cysteine 326 of Solute carrier family 40 member 1
6wbv B 7 A 326
A redox-regulated disulphide may form between cysteine 66 of Hepcidin and cysteine 326 of Solute carrier family 40 member 1 (7 and 326 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
6wbv
Structure name
structure of human ferroportin bound to hepcidin and cobalt in lipid nanodisc
Structure deposition date
2020-03-27
Thiol separation (Å)
8
Half-sphere exposure sum ?
78
Minimum pKa ?
9
% buried
nan
Peptide A name
Hepcidin
Peptide B name
Solute carrier family 40 member 1
Peptide A accession
P81172
Peptide B accession
Q9NP59
Peptide A residue number
66
Peptide B residue number
326
Ligandability
Cysteine 66 of Hepcidin
Cysteine 326 of Solute carrier family 40 member 1
4qae S 23 F 76
A redox-regulated disulphide may form between cysteine 82 of Hepcidin and cysteine 96 of Neutrophil gelatinase-associated lipocalin (23 and 76 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
4qae
Structure name
crystal structure of an engineered lipocalin (anticalin) in complex with human hepcidin
Structure deposition date
2014-05-04
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide A name
Hepcidin
Peptide B name
Neutrophil gelatinase-associated lipocalin
Peptide A accession
P81172
Peptide B accession
P80188
Peptide A residue number
82
Peptide B residue number
96
Ligandability
Cysteine 82 of Hepcidin
Cysteine 96 of Neutrophil gelatinase-associated lipocalin
4qae P 10 B 76
A redox-regulated disulphide may form between cysteine 69 of Hepcidin and cysteine 96 of Neutrophil gelatinase-associated lipocalin (10 and 76 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
4qae
Structure name
crystal structure of an engineered lipocalin (anticalin) in complex with human hepcidin
Structure deposition date
2014-05-04
Thiol separation (Å)
10
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide A name
Hepcidin
Peptide B name
Neutrophil gelatinase-associated lipocalin
Peptide A accession
P81172
Peptide B accession
P80188
Peptide A residue number
69
Peptide B residue number
96
Ligandability
Cysteine 69 of Hepcidin
Cysteine 96 of Neutrophil gelatinase-associated lipocalin
4qae S 13 F 76
A redox-regulated disulphide may form between cysteine 72 of Hepcidin and cysteine 96 of Neutrophil gelatinase-associated lipocalin (13 and 76 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
4qae
Structure name
crystal structure of an engineered lipocalin (anticalin) in complex with human hepcidin
Structure deposition date
2014-05-04
Thiol separation (Å)
10
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide A name
Hepcidin
Peptide B name
Neutrophil gelatinase-associated lipocalin
Peptide A accession
P81172
Peptide B accession
P80188
Peptide A residue number
72
Peptide B residue number
96
Ligandability
Cysteine 72 of Hepcidin
Cysteine 96 of Neutrophil gelatinase-associated lipocalin
3h0t C 11 C 19
A redox-regulated disulphide may form within Hepcidin between cysteines 70 and 78 (11 and 19 respectively in this structure).
Details
Redox score ?
82
PDB code
3h0t
Structure name
hepcidin-fab complex
Structure deposition date
2009-04-10
Thiol separation (Å)
2
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P81172
Residue number A
70
Residue number B
78
Peptide name
Hepcidin
Ligandability
Cysteine 70 of Hepcidin
Cysteine 78 of Hepcidin
4qae Q 7 Q 23
A redox-regulated disulphide may form within Hepcidin between cysteines 66 and 82 (7 and 23 respectively in this structure).
Details
Redox score ?
81
PDB code
4qae
Structure name
crystal structure of an engineered lipocalin (anticalin) in complex with human hepcidin
Structure deposition date
2014-05-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P81172
Residue number A
66
Residue number B
82
Peptide name
Hepcidin
Ligandability
Cysteine 66 of Hepcidin
Cysteine 82 of Hepcidin
3h0t C 13 C 14
A redox-regulated disulphide may form within Hepcidin between cysteines 72 and 73 (13 and 14 respectively in this structure).
Details
Redox score ?
71
PDB code
3h0t
Structure name
hepcidin-fab complex
Structure deposition date
2009-04-10
Thiol separation (Å)
5
Half-sphere exposure sum ?
38
Minimum pKa ?
nan
% buried
nan
Peptide accession
P81172
Residue number A
72
Residue number B
73
Peptide name
Hepcidin
Ligandability
Cysteine 72 of Hepcidin
Cysteine 73 of Hepcidin
3h0t C 13 C 22
A redox-regulated disulphide may form within Hepcidin between cysteines 72 and 81 (13 and 22 respectively in this structure).
Details
Redox score ?
70
PDB code
3h0t
Structure name
hepcidin-fab complex
Structure deposition date
2009-04-10
Thiol separation (Å)
5
Half-sphere exposure sum ?
43
Minimum pKa ?
nan
% buried
nan
Peptide accession
P81172
Residue number A
72
Residue number B
81
Peptide name
Hepcidin
Ligandability
Cysteine 72 of Hepcidin
Cysteine 81 of Hepcidin
4qae T 10 T 22
A redox-regulated disulphide may form within Hepcidin between cysteines 69 and 81 (10 and 22 respectively in this structure).
Details
Redox score ?
67
PDB code
4qae
Structure name
crystal structure of an engineered lipocalin (anticalin) in complex with human hepcidin
Structure deposition date
2014-05-04
Thiol separation (Å)
5
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
P81172
Residue number A
69
Residue number B
81
Peptide name
Hepcidin
Ligandability
Cysteine 69 of Hepcidin
Cysteine 81 of Hepcidin
3h0t C 10 C 14
A redox-regulated disulphide may form within Hepcidin between cysteines 69 and 73 (10 and 14 respectively in this structure).
Details
Redox score ?
66
PDB code
3h0t
Structure name
hepcidin-fab complex
Structure deposition date
2009-04-10
Thiol separation (Å)
5
Half-sphere exposure sum ?
42
Minimum pKa ?
nan
% buried
nan
Peptide accession
P81172
Residue number A
69
Residue number B
73
Peptide name
Hepcidin
Ligandability
Cysteine 69 of Hepcidin
Cysteine 73 of Hepcidin
3h0t C 22 C 23
A redox-regulated disulphide may form within Hepcidin between cysteines 81 and 82 (22 and 23 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
60
PDB code
3h0t
Structure name
hepcidin-fab complex
Structure deposition date
2009-04-10
Thiol separation (Å)
6
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
P81172
Residue number A
81
Residue number B
82
Peptide name
Hepcidin
Ligandability
Cysteine 81 of Hepcidin
Cysteine 82 of Hepcidin
3h0t C 14 C 23
A redox-regulated disulphide may form within Hepcidin between cysteines 73 and 82 (14 and 23 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
3h0t
Structure name
hepcidin-fab complex
Structure deposition date
2009-04-10
Thiol separation (Å)
7
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
P81172
Residue number A
73
Residue number B
82
Peptide name
Hepcidin
Ligandability
Cysteine 73 of Hepcidin
Cysteine 82 of Hepcidin
3h0t C 10 C 11
A redox-regulated disulphide may form within Hepcidin between cysteines 69 and 70 (10 and 11 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
3h0t
Structure name
hepcidin-fab complex
Structure deposition date
2009-04-10
Thiol separation (Å)
7
Half-sphere exposure sum ?
44
Minimum pKa ?
nan
% buried
nan
Peptide accession
P81172
Residue number A
69
Residue number B
70
Peptide name
Hepcidin
Ligandability
Cysteine 69 of Hepcidin
Cysteine 70 of Hepcidin
2kef A 7 A 13
A redox-regulated disulphide may form within Hepcidin between cysteines 66 and 72 (7 and 13 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
2kef
Structure name
solution nmr structures of human hepcidin at 325k
Structure deposition date
2009-01-29
Thiol separation (Å)
9
Half-sphere exposure sum ?
34
Minimum pKa ?
nan
% buried
nan
Peptide accession
P81172
Residue number A
66
Residue number B
72
Peptide name
Hepcidin
Ligandability
Cysteine 66 of Hepcidin
Cysteine 72 of Hepcidin
1m4f A 10 A 13
A redox-regulated disulphide may form within Hepcidin between cysteines 69 and 72 (10 and 13 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
1m4f
Structure name
solution structure of hepcidin-25
Structure deposition date
2002-07-02
Thiol separation (Å)
9
Half-sphere exposure sum ?
29
Minimum pKa ?
nan
% buried
nan
Peptide accession
P81172
Residue number A
69
Residue number B
72
Peptide name
Hepcidin
Ligandability
Cysteine 69 of Hepcidin
Cysteine 72 of Hepcidin
3h0t C 10 C 19
A redox-regulated disulphide may form within Hepcidin between cysteines 69 and 78 (10 and 19 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
3h0t
Structure name
hepcidin-fab complex
Structure deposition date
2009-04-10
Thiol separation (Å)
8
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P81172
Residue number A
69
Residue number B
78
Peptide name
Hepcidin
Ligandability
Cysteine 69 of Hepcidin
Cysteine 78 of Hepcidin
3h0t C 10 C 23
A redox-regulated disulphide may form within Hepcidin between cysteines 69 and 82 (10 and 23 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
3h0t
Structure name
hepcidin-fab complex
Structure deposition date
2009-04-10
Thiol separation (Å)
9
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
P81172
Residue number A
69
Residue number B
82
Peptide name
Hepcidin
Ligandability
Cysteine 69 of Hepcidin
Cysteine 82 of Hepcidin
4qae Q 7 Q 22
A redox-regulated disulphide may form within Hepcidin between cysteines 66 and 81 (7 and 22 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
4qae
Structure name
crystal structure of an engineered lipocalin (anticalin) in complex with human hepcidin
Structure deposition date
2014-05-04
Thiol separation (Å)
9
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
P81172
Residue number A
66
Residue number B
81
Peptide name
Hepcidin
Ligandability
Cysteine 66 of Hepcidin
Cysteine 81 of Hepcidin
1m4e A 6 A 9
A redox-regulated disulphide may form within Hepcidin between cysteines 70 and 73 (6 and 9 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
1m4e
Structure name
solution structure of hepcidin-20
Structure deposition date
2002-07-02
Thiol separation (Å)
9
Half-sphere exposure sum ?
28
Minimum pKa ?
nan
% buried
nan
Peptide accession
P81172
Residue number A
70
Residue number B
73
Peptide name
Hepcidin
Ligandability
Cysteine 70 of Hepcidin
Cysteine 73 of Hepcidin
3h0t C 13 C 23
A redox-regulated disulphide may form within Hepcidin between cysteines 72 and 82 (13 and 23 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
3h0t
Structure name
hepcidin-fab complex
Structure deposition date
2009-04-10
Thiol separation (Å)
10
Half-sphere exposure sum ?
47
Minimum pKa ?
nan
% buried
nan
Peptide accession
P81172
Residue number A
72
Residue number B
82
Peptide name
Hepcidin
Ligandability
Cysteine 72 of Hepcidin
Cysteine 82 of Hepcidin
4qae U 11 U 22
A redox-regulated disulphide may form within Hepcidin between cysteines 70 and 81 (11 and 22 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
4qae
Structure name
crystal structure of an engineered lipocalin (anticalin) in complex with human hepcidin
Structure deposition date
2014-05-04
Thiol separation (Å)
9
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P81172
Residue number A
70
Residue number B
81
Peptide name
Hepcidin
Ligandability
Cysteine 70 of Hepcidin
Cysteine 81 of Hepcidin
4qae T 19 T 22
A redox-regulated disulphide may form within Hepcidin between cysteines 78 and 81 (19 and 22 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
4qae
Structure name
crystal structure of an engineered lipocalin (anticalin) in complex with human hepcidin
Structure deposition date
2014-05-04
Thiol separation (Å)
9
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide accession
P81172
Residue number A
78
Residue number B
81
Peptide name
Hepcidin
Ligandability
Cysteine 78 of Hepcidin
Cysteine 81 of Hepcidin
4qae Q 11 Q 13
A redox-regulated disulphide may form within Hepcidin between cysteines 70 and 72 (11 and 13 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
4qae
Structure name
crystal structure of an engineered lipocalin (anticalin) in complex with human hepcidin
Structure deposition date
2014-05-04
Thiol separation (Å)
9
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
P81172
Residue number A
70
Residue number B
72
Peptide name
Hepcidin
Ligandability
Cysteine 70 of Hepcidin
Cysteine 72 of Hepcidin
1m4f A 14 A 22
A redox-regulated disulphide may form within Hepcidin between cysteines 73 and 81 (14 and 22 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
1m4f
Structure name
solution structure of hepcidin-25
Structure deposition date
2002-07-02
Thiol separation (Å)
10
Half-sphere exposure sum ?
27
Minimum pKa ?
nan
% buried
nan
Peptide accession
P81172
Residue number A
73
Residue number B
81
Peptide name
Hepcidin
Ligandability
Cysteine 73 of Hepcidin
Cysteine 81 of Hepcidin
1m4e A 9 A 14
A redox-regulated disulphide may form within Hepcidin between cysteines 73 and 78 (9 and 14 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
1m4e
Structure name
solution structure of hepcidin-20
Structure deposition date
2002-07-02
Thiol separation (Å)
10
Half-sphere exposure sum ?
28
Minimum pKa ?
nan
% buried
nan
Peptide accession
P81172
Residue number A
73
Residue number B
78
Peptide name
Hepcidin
Ligandability
Cysteine 73 of Hepcidin
Cysteine 78 of Hepcidin
4qae U 7 U 14
A redox-regulated disulphide may form within Hepcidin between cysteines 66 and 73 (7 and 14 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
4qae
Structure name
crystal structure of an engineered lipocalin (anticalin) in complex with human hepcidin
Structure deposition date
2014-05-04
Thiol separation (Å)
9
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P81172
Residue number A
66
Residue number B
73
Peptide name
Hepcidin
Ligandability
Cysteine 66 of Hepcidin
Cysteine 73 of Hepcidin
3h0t C 7 C 10
A redox-regulated disulphide may form within Hepcidin between cysteines 66 and 69 (7 and 10 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
3h0t
Structure name
hepcidin-fab complex
Structure deposition date
2009-04-10
Thiol separation (Å)
10
Half-sphere exposure sum ?
46
Minimum pKa ?
nan
% buried
nan
Peptide accession
P81172
Residue number A
66
Residue number B
69
Peptide name
Hepcidin
Ligandability
Cysteine 66 of Hepcidin
Cysteine 69 of Hepcidin
4qae U 13 U 19
A redox-regulated disulphide may form within Hepcidin between cysteines 72 and 78 (13 and 19 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
36
PDB code
4qae
Structure name
crystal structure of an engineered lipocalin (anticalin) in complex with human hepcidin
Structure deposition date
2014-05-04
Thiol separation (Å)
10
Half-sphere exposure sum ?
84
Minimum pKa ?
nan
% buried
nan
Peptide accession
P81172
Residue number A
72
Residue number B
78
Peptide name
Hepcidin
Ligandability
Cysteine 72 of Hepcidin
Cysteine 78 of Hepcidin
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