Zinc finger FYVE domain-containing protein 9
Intermolecular
Cysteine 338 of Mothers against decapentaplegic homolog 3 and cysteine 783
Cysteine 380 of Mothers against decapentaplegic homolog 2 and cysteine 783
Cysteine 374 of Mothers against decapentaplegic homolog 2 and cysteine 783
Cysteine 332 of Mothers against decapentaplegic homolog 3 and cysteine 783
Cysteine 320 of Mothers against decapentaplegic homolog 3 and cysteine 783
Cysteine 362 of Mothers against decapentaplegic homolog 2 and cysteine 783
Cysteine 349 of Mothers against decapentaplegic homolog 2 and cysteine 783
Cysteine 307 of Mothers against decapentaplegic homolog 3 and cysteine 783
Intramolecular
Cysteine 962 and cysteine 984
Cysteine 1344 and cysteine 1348
Cysteine 962 and cysteine 964
1mk2 A 337 B 681
A redox-regulated disulphide may form between cysteine 338 of Mothers against decapentaplegic homolog 3 and cysteine 783 of Zinc finger FYVE domain-containing protein 9 (337 and 681 respectively in this structure).
Details
Redox score ?
63
PDB code
1mk2
Structure name
smad3 sbd complex
Structure deposition date
2002-08-28
Thiol separation (Å)
5
Half-sphere exposure sum ?
65
Minimum pKa ?
10
% buried
46
Peptide A name
Mothers against decapentaplegic homolog 3
Peptide B name
Zinc finger FYVE domain-containing protein 9
Peptide A accession
P84022
Peptide B accession
O95405
Peptide A residue number
338
Peptide B residue number
783
Ligandability
Cysteine 338 of Mothers against decapentaplegic homolog 3
Cysteine 783 of Zinc finger FYVE domain-containing protein 9
1dev C 380 D 681
A redox-regulated disulphide may form between cysteine 380 of Mothers against decapentaplegic homolog 2 and cysteine 783 of Zinc finger FYVE domain-containing protein 9 (380 and 681 respectively in this structure).
Details
Redox score ?
60
PDB code
1dev
Structure name
crystal structure of smad2 mh2 domain bound to the smad-binding domain of sara
Structure deposition date
1999-11-15
Thiol separation (Å)
6
Half-sphere exposure sum ?
66
Minimum pKa ?
10
% buried
48
Peptide A name
Mothers against decapentaplegic homolog 2
Peptide B name
Zinc finger FYVE domain-containing protein 9
Peptide A accession
Q15796
Peptide B accession
O95405
Peptide A residue number
380
Peptide B residue number
783
Ligandability
Cysteine 380 of Mothers against decapentaplegic homolog 2
Cysteine 783 of Zinc finger FYVE domain-containing protein 9
1dev A 374 B 681
A redox-regulated disulphide may form between cysteine 374 of Mothers against decapentaplegic homolog 2 and cysteine 783 of Zinc finger FYVE domain-containing protein 9 (374 and 681 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
1dev
Structure name
crystal structure of smad2 mh2 domain bound to the smad-binding domain of sara
Structure deposition date
1999-11-15
Thiol separation (Å)
6
Half-sphere exposure sum ?
82
Minimum pKa ?
13
% buried
86
Peptide A name
Mothers against decapentaplegic homolog 2
Peptide B name
Zinc finger FYVE domain-containing protein 9
Peptide A accession
Q15796
Peptide B accession
O95405
Peptide A residue number
374
Peptide B residue number
783
Ligandability
Cysteine 374 of Mothers against decapentaplegic homolog 2
Cysteine 783 of Zinc finger FYVE domain-containing protein 9
1mk2 A 331 B 681
A redox-regulated disulphide may form between cysteine 332 of Mothers against decapentaplegic homolog 3 and cysteine 783 of Zinc finger FYVE domain-containing protein 9 (331 and 681 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
1mk2
Structure name
smad3 sbd complex
Structure deposition date
2002-08-28
Thiol separation (Å)
6
Half-sphere exposure sum ?
79
Minimum pKa ?
12
% buried
84
Peptide A name
Mothers against decapentaplegic homolog 3
Peptide B name
Zinc finger FYVE domain-containing protein 9
Peptide A accession
P84022
Peptide B accession
O95405
Peptide A residue number
332
Peptide B residue number
783
Ligandability
Cysteine 332 of Mothers against decapentaplegic homolog 3
Cysteine 783 of Zinc finger FYVE domain-containing protein 9
1mk2 A 319 B 681
A redox-regulated disulphide may form between cysteine 320 of Mothers against decapentaplegic homolog 3 and cysteine 783 of Zinc finger FYVE domain-containing protein 9 (319 and 681 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
1mk2
Structure name
smad3 sbd complex
Structure deposition date
2002-08-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
10
% buried
84
Peptide A name
Mothers against decapentaplegic homolog 3
Peptide B name
Zinc finger FYVE domain-containing protein 9
Peptide A accession
P84022
Peptide B accession
O95405
Peptide A residue number
320
Peptide B residue number
783
Ligandability
Cysteine 320 of Mothers against decapentaplegic homolog 3
Cysteine 783 of Zinc finger FYVE domain-containing protein 9
1dev A 362 B 681
A redox-regulated disulphide may form between cysteine 362 of Mothers against decapentaplegic homolog 2 and cysteine 783 of Zinc finger FYVE domain-containing protein 9 (362 and 681 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
1dev
Structure name
crystal structure of smad2 mh2 domain bound to the smad-binding domain of sara
Structure deposition date
1999-11-15
Thiol separation (Å)
9
Half-sphere exposure sum ?
76
Minimum pKa ?
10
% buried
86
Peptide A name
Mothers against decapentaplegic homolog 2
Peptide B name
Zinc finger FYVE domain-containing protein 9
Peptide A accession
Q15796
Peptide B accession
O95405
Peptide A residue number
362
Peptide B residue number
783
Ligandability
Cysteine 362 of Mothers against decapentaplegic homolog 2
Cysteine 783 of Zinc finger FYVE domain-containing protein 9
1dev C 349 D 681
A redox-regulated disulphide may form between cysteine 349 of Mothers against decapentaplegic homolog 2 and cysteine 783 of Zinc finger FYVE domain-containing protein 9 (349 and 681 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
1dev
Structure name
crystal structure of smad2 mh2 domain bound to the smad-binding domain of sara
Structure deposition date
1999-11-15
Thiol separation (Å)
9
Half-sphere exposure sum ?
75
Minimum pKa ?
11
% buried
68
Peptide A name
Mothers against decapentaplegic homolog 2
Peptide B name
Zinc finger FYVE domain-containing protein 9
Peptide A accession
Q15796
Peptide B accession
O95405
Peptide A residue number
349
Peptide B residue number
783
Ligandability
Cysteine 349 of Mothers against decapentaplegic homolog 2
Cysteine 783 of Zinc finger FYVE domain-containing protein 9
1mk2 A 306 B 681
A redox-regulated disulphide may form between cysteine 307 of Mothers against decapentaplegic homolog 3 and cysteine 783 of Zinc finger FYVE domain-containing protein 9 (306 and 681 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
1mk2
Structure name
smad3 sbd complex
Structure deposition date
2002-08-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
75
Minimum pKa ?
12
% buried
68
Peptide A name
Mothers against decapentaplegic homolog 3
Peptide B name
Zinc finger FYVE domain-containing protein 9
Peptide A accession
P84022
Peptide B accession
O95405
Peptide A residue number
307
Peptide B residue number
783
Ligandability
Cysteine 307 of Mothers against decapentaplegic homolog 3
Cysteine 783 of Zinc finger FYVE domain-containing protein 9
4bkw A 962 A 984
A redox-regulated disulphide may form within Zinc finger FYVE domain-containing protein 9 between cysteines 962 and 984. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
57
PDB code
4bkw
Structure name
crystal structure of the c-terminal region of human zfyve9
Structure deposition date
2013-04-30
Thiol separation (Å)
6
Half-sphere exposure sum ?
59
Minimum pKa ?
11
% buried
53
Peptide accession
O95405
Residue number A
962
Residue number B
984
Peptide name
Zinc finger FYVE domain-containing protein 9
Ligandability
Cysteine 962 of Zinc finger FYVE domain-containing protein 9
Cysteine 984 of Zinc finger FYVE domain-containing protein 9
4bkw A 1344 A 1348
A redox-regulated disulphide may form within Zinc finger FYVE domain-containing protein 9 between cysteines 1344 and 1348. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
54
PDB code
4bkw
Structure name
crystal structure of the c-terminal region of human zfyve9
Structure deposition date
2013-04-30
Thiol separation (Å)
7
Half-sphere exposure sum ?
68
Minimum pKa ?
10
% buried
57
Peptide accession
O95405
Residue number A
1344
Residue number B
1348
Peptide name
Zinc finger FYVE domain-containing protein 9
Ligandability
Cysteine 1344 of Zinc finger FYVE domain-containing protein 9
Cysteine 1348 of Zinc finger FYVE domain-containing protein 9
4bkw A 962 A 964
A redox-regulated disulphide may form within Zinc finger FYVE domain-containing protein 9 between cysteines 962 and 964. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
4bkw
Structure name
crystal structure of the c-terminal region of human zfyve9
Structure deposition date
2013-04-30
Thiol separation (Å)
8
Half-sphere exposure sum ?
72
Minimum pKa ?
12
% buried
78
Peptide accession
O95405
Residue number A
962
Residue number B
964
Peptide name
Zinc finger FYVE domain-containing protein 9
Ligandability
Cysteine 962 of Zinc finger FYVE domain-containing protein 9
Cysteine 964 of Zinc finger FYVE domain-containing protein 9
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