ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Hepatocyte growth factor receptor

Intermolecular
Cysteine 584 and cysteine 26
Intramolecular
Cysteine 95 and cysteine 101
Cysteine 541 and cysteine 551
Cysteine 385 and cysteine 397
Cysteine 697 and cysteine 709
Cysteine 520 and cysteine 538
Cysteine 282 and cysteine 172
Cysteine 529 and cysteine 545
Cysteine 98 and cysteine 160
Cysteine 282 and cysteine 409
More...
Cysteine 172 and cysteine 175
Cysteine 298 and cysteine 363
Cysteine 526 and cysteine 561
Cysteine 133 and cysteine 141
Cysteine 520 and cysteine 545
Cysteine 610 and cysteine 624
Cysteine 538 and cysteine 545
Cysteine 529 and cysteine 538
Cysteine 520 and cysteine 529
Cysteine 526 and cysteine 529
Cysteine 529 and cysteine 561
Cysteine 538 and cysteine 551
Cysteine 526 and cysteine 545
Cysteine 520 and cysteine 526
Cysteine 538 and cysteine 541
Cysteine 98 and cysteine 141
Cysteine 520 and cysteine 551
Cysteine 529 and cysteine 551
Cysteine 545 and cysteine 551
Cysteine 98 and cysteine 175
Cysteine 141 and cysteine 160
Cysteine 98 and cysteine 101
Cysteine 520 and cysteine 541
Cysteine 545 and cysteine 561
Cysteine 98 and cysteine 172
Cysteine 1107 and cysteine 1146
Cysteine 95 and cysteine 98
Cysteine 529 and cysteine 541
Cysteine 541 and cysteine 545
Cysteine 526 and cysteine 541
A redox-regulated disulphide may form between two units of Hepatocyte growth factor receptor at cysteines 584 and 26.

Details

Redox score ?
85
PDB code
5lsp
Structure name
107_a07 fab in complex with fragment of the met receptor
Structure deposition date
2016-09-05
Thiol separation (Å)
2
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide A name
Hepatocyte growth factor receptor
Peptide B name
Hepatocyte growth factor receptor
Peptide A accession
P08581
Peptide B accession
P08581
Peptide A residue number
584
Peptide B residue number
26

Ligandability

Cysteine 584 of Hepatocyte growth factor receptor

Cysteine 26 of Hepatocyte growth factor receptor

A redox-regulated disulphide may form within Hepatocyte growth factor receptor between cysteines 95 and 101.

Details

Redox score ?
89
PDB code
4o3u
Structure name
zymogen hgf-beta/met with zymogen activator peptide zap2
Structure deposition date
2013-12-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
45
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08581
Residue number A
95
Residue number B
101
Peptide name
Hepatocyte growth factor receptor

Ligandability

Cysteine 95 of Hepatocyte growth factor receptor

Cysteine 101 of Hepatocyte growth factor receptor

A redox-regulated disulphide may form within Hepatocyte growth factor receptor between cysteines 541 and 551.

Details

Redox score ?
87
PDB code
2uzx
Structure name
structure of the human receptor tyrosine kinase met in complex with the listeria monocytogenes invasion protein inlb: crystal form i
Structure deposition date
2007-05-02
Thiol separation (Å)
2
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08581
Residue number A
541
Residue number B
551
Peptide name
Hepatocyte growth factor receptor

Ligandability

Cysteine 541 of Hepatocyte growth factor receptor

Cysteine 551 of Hepatocyte growth factor receptor

A redox-regulated disulphide may form within Hepatocyte growth factor receptor between cysteines 385 and 397.

Details

Redox score ?
86
PDB code
6gcu
Structure name
met receptor in complex with inlb internalin domain and darpin a3a
Structure deposition date
2018-04-19
Thiol separation (Å)
2
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08581
Residue number A
385
Residue number B
397
Peptide name
Hepatocyte growth factor receptor

Ligandability

Cysteine 385 of Hepatocyte growth factor receptor

Cysteine 397 of Hepatocyte growth factor receptor

A redox-regulated disulphide may form within Hepatocyte growth factor receptor between cysteines 697 and 709.

Details

Redox score ?
86
PDB code
5lsp
Structure name
107_a07 fab in complex with fragment of the met receptor
Structure deposition date
2016-09-05
Thiol separation (Å)
2
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08581
Residue number A
697
Residue number B
709
Peptide name
Hepatocyte growth factor receptor

Ligandability

Cysteine 697 of Hepatocyte growth factor receptor

Cysteine 709 of Hepatocyte growth factor receptor

A redox-regulated disulphide may form within Hepatocyte growth factor receptor between cysteines 520 and 538.

Details

Redox score ?
86
PDB code
2uzx
Structure name
structure of the human receptor tyrosine kinase met in complex with the listeria monocytogenes invasion protein inlb: crystal form i
Structure deposition date
2007-05-02
Thiol separation (Å)
2
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08581
Residue number A
520
Residue number B
538
Peptide name
Hepatocyte growth factor receptor

Ligandability

Cysteine 520 of Hepatocyte growth factor receptor

Cysteine 538 of Hepatocyte growth factor receptor

A redox-regulated disulphide may form within Hepatocyte growth factor receptor between cysteines 282 and 172 (282 and 409 respectively in this structure).

Details

Redox score ?
85
PDB code
2uzy
Structure name
structure of the human receptor tyrosine kinase met in complex with the listeria monocytogenes invasion protein inlb: low resolution, crystal form ii
Structure deposition date
2007-05-02
Thiol separation (Å)
2
Half-sphere exposure sum ?
45
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08581
Residue number A
282
Residue number B
172
Peptide name
Hepatocyte growth factor receptor

Ligandability

Cysteine 282 of Hepatocyte growth factor receptor

Cysteine 172 of Hepatocyte growth factor receptor

Uncertain whether structure cysteine 409 has been assigned to correct residue.
A redox-regulated disulphide may form within Hepatocyte growth factor receptor between cysteines 529 and 545.

Details

Redox score ?
84
PDB code
5lsp
Structure name
107_a07 fab in complex with fragment of the met receptor
Structure deposition date
2016-09-05
Thiol separation (Å)
2
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08581
Residue number A
529
Residue number B
545
Peptide name
Hepatocyte growth factor receptor

Ligandability

Cysteine 529 of Hepatocyte growth factor receptor

Cysteine 545 of Hepatocyte growth factor receptor

A redox-regulated disulphide may form within Hepatocyte growth factor receptor between cysteines 98 and 160.

Details

Redox score ?
83
PDB code
4o3t
Structure name
zymogen hgf-beta/met with zymogen activator peptide zap
Structure deposition date
2013-12-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08581
Residue number A
98
Residue number B
160
Peptide name
Hepatocyte growth factor receptor

Ligandability

Cysteine 98 of Hepatocyte growth factor receptor

Cysteine 160 of Hepatocyte growth factor receptor

A redox-regulated disulphide may form within Hepatocyte growth factor receptor between cysteines 282 and 409.

Details

Redox score ?
83
PDB code
6wvz
Structure name
crystal structure of anti-met fab arm of amivantamab in complex with human met
Structure deposition date
2020-05-07
Thiol separation (Å)
2
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08581
Residue number A
282
Residue number B
409
Peptide name
Hepatocyte growth factor receptor

Ligandability

Cysteine 282 of Hepatocyte growth factor receptor

Cysteine 409 of Hepatocyte growth factor receptor

A redox-regulated disulphide may form within Hepatocyte growth factor receptor between cysteines 172 and 175.

Details

Redox score ?
82
PDB code
2uzy
Structure name
structure of the human receptor tyrosine kinase met in complex with the listeria monocytogenes invasion protein inlb: low resolution, crystal form ii
Structure deposition date
2007-05-02
Thiol separation (Å)
2
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08581
Residue number A
172
Residue number B
175
Peptide name
Hepatocyte growth factor receptor

Ligandability

Cysteine 172 of Hepatocyte growth factor receptor

Cysteine 175 of Hepatocyte growth factor receptor

A redox-regulated disulphide may form within Hepatocyte growth factor receptor between cysteines 298 and 363.

Details

Redox score ?
80
PDB code
6wvz
Structure name
crystal structure of anti-met fab arm of amivantamab in complex with human met
Structure deposition date
2020-05-07
Thiol separation (Å)
2
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08581
Residue number A
298
Residue number B
363
Peptide name
Hepatocyte growth factor receptor

Ligandability

Cysteine 298 of Hepatocyte growth factor receptor

Cysteine 363 of Hepatocyte growth factor receptor

A redox-regulated disulphide may form within Hepatocyte growth factor receptor between cysteines 526 and 561.

Details

Redox score ?
79
PDB code
6gcu
Structure name
met receptor in complex with inlb internalin domain and darpin a3a
Structure deposition date
2018-04-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
nan
Minimum pKa ?
8
% buried
61
Peptide accession
P08581
Residue number A
526
Residue number B
561
Peptide name
Hepatocyte growth factor receptor

Ligandability

Cysteine 526 of Hepatocyte growth factor receptor

Cysteine 561 of Hepatocyte growth factor receptor

A redox-regulated disulphide may form within Hepatocyte growth factor receptor between cysteines 133 and 141.

Details

Redox score ?
78
PDB code
2uzy
Structure name
structure of the human receptor tyrosine kinase met in complex with the listeria monocytogenes invasion protein inlb: low resolution, crystal form ii
Structure deposition date
2007-05-02
Thiol separation (Å)
2
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08581
Residue number A
133
Residue number B
141
Peptide name
Hepatocyte growth factor receptor

Ligandability

Cysteine 133 of Hepatocyte growth factor receptor

Cysteine 141 of Hepatocyte growth factor receptor

A redox-regulated disulphide may form within Hepatocyte growth factor receptor between cysteines 520 and 545.

Details

Redox score ?
73
PDB code
6gcu
Structure name
met receptor in complex with inlb internalin domain and darpin a3a
Structure deposition date
2018-04-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08581
Residue number A
520
Residue number B
545
Peptide name
Hepatocyte growth factor receptor

Ligandability

Cysteine 520 of Hepatocyte growth factor receptor

Cysteine 545 of Hepatocyte growth factor receptor

A redox-regulated disulphide may form within Hepatocyte growth factor receptor between cysteines 610 and 624.

Details

Redox score ?
71
PDB code
6gcu
Structure name
met receptor in complex with inlb internalin domain and darpin a3a
Structure deposition date
2018-04-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
8
% buried
92
Peptide accession
P08581
Residue number A
610
Residue number B
624
Peptide name
Hepatocyte growth factor receptor

Ligandability

Cysteine 610 of Hepatocyte growth factor receptor

Cysteine 624 of Hepatocyte growth factor receptor

A redox-regulated disulphide may form within Hepatocyte growth factor receptor between cysteines 538 and 545.

Details

Redox score ?
71
PDB code
2uzy
Structure name
structure of the human receptor tyrosine kinase met in complex with the listeria monocytogenes invasion protein inlb: low resolution, crystal form ii
Structure deposition date
2007-05-02
Thiol separation (Å)
4
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08581
Residue number A
538
Residue number B
545
Peptide name
Hepatocyte growth factor receptor

Ligandability

Cysteine 538 of Hepatocyte growth factor receptor

Cysteine 545 of Hepatocyte growth factor receptor

A redox-regulated disulphide may form within Hepatocyte growth factor receptor between cysteines 529 and 538.

Details

Redox score ?
66
PDB code
2uzy
Structure name
structure of the human receptor tyrosine kinase met in complex with the listeria monocytogenes invasion protein inlb: low resolution, crystal form ii
Structure deposition date
2007-05-02
Thiol separation (Å)
5
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08581
Residue number A
529
Residue number B
538
Peptide name
Hepatocyte growth factor receptor

Ligandability

Cysteine 529 of Hepatocyte growth factor receptor

Cysteine 538 of Hepatocyte growth factor receptor

A redox-regulated disulphide may form within Hepatocyte growth factor receptor between cysteines 520 and 529.

Details

Redox score ?
61
PDB code
5lsp
Structure name
107_a07 fab in complex with fragment of the met receptor
Structure deposition date
2016-09-05
Thiol separation (Å)
7
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08581
Residue number A
520
Residue number B
529
Peptide name
Hepatocyte growth factor receptor

Ligandability

Cysteine 520 of Hepatocyte growth factor receptor

Cysteine 529 of Hepatocyte growth factor receptor

A redox-regulated disulphide may form within Hepatocyte growth factor receptor between cysteines 526 and 529.

Details

Redox score ?
60
PDB code
1shy
Structure name
the crystal structure of hgf beta-chain in complex with the sema domain of the met receptor
Structure deposition date
2004-02-26
Thiol separation (Å)
6
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08581
Residue number A
526
Residue number B
529
Peptide name
Hepatocyte growth factor receptor

Ligandability

Cysteine 526 of Hepatocyte growth factor receptor

Cysteine 529 of Hepatocyte growth factor receptor

A redox-regulated disulphide may form within Hepatocyte growth factor receptor between cysteines 529 and 561. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
4k3j
Structure name
crystal structure of onartuzumab fab in complex with met and hgf-beta
Structure deposition date
2013-04-10
Thiol separation (Å)
8
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08581
Residue number A
529
Residue number B
561
Peptide name
Hepatocyte growth factor receptor

Ligandability

Cysteine 529 of Hepatocyte growth factor receptor

Cysteine 561 of Hepatocyte growth factor receptor

A redox-regulated disulphide may form within Hepatocyte growth factor receptor between cysteines 538 and 551 (24 and 37 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
1ssl
Structure name
solution structure of the psi domain from the met receptor
Structure deposition date
2004-03-24
Thiol separation (Å)
8
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08581
Residue number A
538
Residue number B
551
Peptide name
Hepatocyte growth factor receptor

Ligandability

Cysteine 538 of Hepatocyte growth factor receptor

Cysteine 551 of Hepatocyte growth factor receptor

A redox-regulated disulphide may form within Hepatocyte growth factor receptor between cysteines 526 and 545. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
6wvz
Structure name
crystal structure of anti-met fab arm of amivantamab in complex with human met
Structure deposition date
2020-05-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08581
Residue number A
526
Residue number B
545
Peptide name
Hepatocyte growth factor receptor

Ligandability

Cysteine 526 of Hepatocyte growth factor receptor

Cysteine 545 of Hepatocyte growth factor receptor

A redox-regulated disulphide may form within Hepatocyte growth factor receptor between cysteines 520 and 526 (6 and 12 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
1ssl
Structure name
solution structure of the psi domain from the met receptor
Structure deposition date
2004-03-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08581
Residue number A
520
Residue number B
526
Peptide name
Hepatocyte growth factor receptor

Ligandability

Cysteine 520 of Hepatocyte growth factor receptor

Cysteine 526 of Hepatocyte growth factor receptor

A redox-regulated disulphide may form within Hepatocyte growth factor receptor between cysteines 538 and 541 (24 and 27 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
1ssl
Structure name
solution structure of the psi domain from the met receptor
Structure deposition date
2004-03-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08581
Residue number A
538
Residue number B
541
Peptide name
Hepatocyte growth factor receptor

Ligandability

Cysteine 538 of Hepatocyte growth factor receptor

Cysteine 541 of Hepatocyte growth factor receptor

A redox-regulated disulphide may form within Hepatocyte growth factor receptor between cysteines 98 and 141. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
4o3t
Structure name
zymogen hgf-beta/met with zymogen activator peptide zap
Structure deposition date
2013-12-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08581
Residue number A
98
Residue number B
141
Peptide name
Hepatocyte growth factor receptor

Ligandability

Cysteine 98 of Hepatocyte growth factor receptor

Cysteine 141 of Hepatocyte growth factor receptor

A redox-regulated disulphide may form within Hepatocyte growth factor receptor between cysteines 520 and 551 (6 and 37 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
1ssl
Structure name
solution structure of the psi domain from the met receptor
Structure deposition date
2004-03-24
Thiol separation (Å)
10
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08581
Residue number A
520
Residue number B
551
Peptide name
Hepatocyte growth factor receptor

Ligandability

Cysteine 520 of Hepatocyte growth factor receptor

Cysteine 551 of Hepatocyte growth factor receptor

A redox-regulated disulphide may form within Hepatocyte growth factor receptor between cysteines 529 and 551. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
6wvz
Structure name
crystal structure of anti-met fab arm of amivantamab in complex with human met
Structure deposition date
2020-05-07
Thiol separation (Å)
10
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08581
Residue number A
529
Residue number B
551
Peptide name
Hepatocyte growth factor receptor

Ligandability

Cysteine 529 of Hepatocyte growth factor receptor

Cysteine 551 of Hepatocyte growth factor receptor

A redox-regulated disulphide may form within Hepatocyte growth factor receptor between cysteines 545 and 551. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
2uzy
Structure name
structure of the human receptor tyrosine kinase met in complex with the listeria monocytogenes invasion protein inlb: low resolution, crystal form ii
Structure deposition date
2007-05-02
Thiol separation (Å)
10
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08581
Residue number A
545
Residue number B
551
Peptide name
Hepatocyte growth factor receptor

Ligandability

Cysteine 545 of Hepatocyte growth factor receptor

Cysteine 551 of Hepatocyte growth factor receptor

A redox-regulated disulphide may form within Hepatocyte growth factor receptor between cysteines 98 and 175. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
4o3u
Structure name
zymogen hgf-beta/met with zymogen activator peptide zap2
Structure deposition date
2013-12-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08581
Residue number A
98
Residue number B
175
Peptide name
Hepatocyte growth factor receptor

Ligandability

Cysteine 98 of Hepatocyte growth factor receptor

Cysteine 175 of Hepatocyte growth factor receptor

A redox-regulated disulphide may form within Hepatocyte growth factor receptor between cysteines 141 and 160. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
1shy
Structure name
the crystal structure of hgf beta-chain in complex with the sema domain of the met receptor
Structure deposition date
2004-02-26
Thiol separation (Å)
9
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08581
Residue number A
141
Residue number B
160
Peptide name
Hepatocyte growth factor receptor

Ligandability

Cysteine 141 of Hepatocyte growth factor receptor

Cysteine 160 of Hepatocyte growth factor receptor

A redox-regulated disulphide may form within Hepatocyte growth factor receptor between cysteines 98 and 101. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
7mo7
Structure name
cryo-em structure of 2:2 c-met/hgf holo-complex
Structure deposition date
2021-05-01
Thiol separation (Å)
10
Half-sphere exposure sum ?
47
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08581
Residue number A
98
Residue number B
101
Peptide name
Hepatocyte growth factor receptor

Ligandability

Cysteine 98 of Hepatocyte growth factor receptor

Cysteine 101 of Hepatocyte growth factor receptor

A redox-regulated disulphide may form within Hepatocyte growth factor receptor between cysteines 520 and 541 (6 and 27 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
1ssl
Structure name
solution structure of the psi domain from the met receptor
Structure deposition date
2004-03-24
Thiol separation (Å)
10
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08581
Residue number A
520
Residue number B
541
Peptide name
Hepatocyte growth factor receptor

Ligandability

Cysteine 520 of Hepatocyte growth factor receptor

Cysteine 541 of Hepatocyte growth factor receptor

A redox-regulated disulphide may form within Hepatocyte growth factor receptor between cysteines 545 and 561. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
5lsp
Structure name
107_a07 fab in complex with fragment of the met receptor
Structure deposition date
2016-09-05
Thiol separation (Å)
10
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08581
Residue number A
545
Residue number B
561
Peptide name
Hepatocyte growth factor receptor

Ligandability

Cysteine 545 of Hepatocyte growth factor receptor

Cysteine 561 of Hepatocyte growth factor receptor

A redox-regulated disulphide may form within Hepatocyte growth factor receptor between cysteines 98 and 172. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
4o3t
Structure name
zymogen hgf-beta/met with zymogen activator peptide zap
Structure deposition date
2013-12-18
Thiol separation (Å)
10
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08581
Residue number A
98
Residue number B
172
Peptide name
Hepatocyte growth factor receptor

Ligandability

Cysteine 98 of Hepatocyte growth factor receptor

Cysteine 172 of Hepatocyte growth factor receptor

A redox-regulated disulphide may form within Hepatocyte growth factor receptor between cysteines 1107 and 1146. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
5t3q
Structure name
crystal structure of the c-met kinase domain in complex with a pyrazolone inhibitor
Structure deposition date
2016-08-26
Thiol separation (Å)
9
Half-sphere exposure sum ?
71
Minimum pKa ?
11
% buried
67
Peptide accession
P08581
Residue number A
1107
Residue number B
1146
Peptide name
Hepatocyte growth factor receptor

Ligandability

Cysteine 1107 of Hepatocyte growth factor receptor

Cysteine 1146 of Hepatocyte growth factor receptor

A redox-regulated disulphide may form within Hepatocyte growth factor receptor between cysteines 95 and 98. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
6i04
Structure name
crystal structure of sema domain of the met receptor in complex with fab
Structure deposition date
2018-10-25
Thiol separation (Å)
10
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08581
Residue number A
95
Residue number B
98
Peptide name
Hepatocyte growth factor receptor

Ligandability

Cysteine 95 of Hepatocyte growth factor receptor

Cysteine 98 of Hepatocyte growth factor receptor

A redox-regulated disulphide may form within Hepatocyte growth factor receptor between cysteines 529 and 541. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
4o3t
Structure name
zymogen hgf-beta/met with zymogen activator peptide zap
Structure deposition date
2013-12-18
Thiol separation (Å)
10
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08581
Residue number A
529
Residue number B
541
Peptide name
Hepatocyte growth factor receptor

Ligandability

Cysteine 529 of Hepatocyte growth factor receptor

Cysteine 541 of Hepatocyte growth factor receptor

A redox-regulated disulphide may form within Hepatocyte growth factor receptor between cysteines 541 and 545. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
1shy
Structure name
the crystal structure of hgf beta-chain in complex with the sema domain of the met receptor
Structure deposition date
2004-02-26
Thiol separation (Å)
10
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08581
Residue number A
541
Residue number B
545
Peptide name
Hepatocyte growth factor receptor

Ligandability

Cysteine 541 of Hepatocyte growth factor receptor

Cysteine 545 of Hepatocyte growth factor receptor

A redox-regulated disulphide may form within Hepatocyte growth factor receptor between cysteines 526 and 541. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
7mo7
Structure name
cryo-em structure of 2:2 c-met/hgf holo-complex
Structure deposition date
2021-05-01
Thiol separation (Å)
10
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08581
Residue number A
526
Residue number B
541
Peptide name
Hepatocyte growth factor receptor

Ligandability

Cysteine 526 of Hepatocyte growth factor receptor

Cysteine 541 of Hepatocyte growth factor receptor

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