Zinc finger MYND domain-containing protein 11
Intermolecular
Cysteine 528 and cysteine 528
Cysteine 535 and cysteine 535
Cysteine 528 and cysteine 535
Intramolecular
Cysteine 575 and cysteine 598
Cysteine 574 and cysteine 575
Cysteine 563 and cysteine 585
Cysteine 581 and cysteine 585
Cysteine 574 and cysteine 598
Cysteine 258 and cysteine 277
Cysteine 258 and cysteine 261
More...Cysteine 566 and cysteine 585
Cysteine 563 and cysteine 566
Cysteine 566 and cysteine 581
Cysteine 563 and cysteine 581
Cysteine 261 and cysteine 277
5hda A 488 C 488
A redox-regulated disulphide may form between two units of Zinc finger MYND domain-containing protein 11 at cysteines 528 and 528 (488 and 488 respectively in this structure).
Details
Redox score ?
78
PDB code
5hda
Structure name
crystal structure of the bs69 coiled coil-mynd domains bound to an ebna2 pxlxp motif
Structure deposition date
2016-01-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
9
% buried
0
Peptide A name
Zinc finger MYND domain-containing protein 11
Peptide B name
Zinc finger MYND domain-containing protein 11
Peptide A accession
Q15326
Peptide B accession
Q15326
Peptide A residue number
528
Peptide B residue number
528
Ligandability
5hda A 495 C 495
A redox-regulated disulphide may form between two units of Zinc finger MYND domain-containing protein 11 at cysteines 535 and 535 (495 and 495 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
58
PDB code
5hda
Structure name
crystal structure of the bs69 coiled coil-mynd domains bound to an ebna2 pxlxp motif
Structure deposition date
2016-01-05
Thiol separation (Å)
7
Half-sphere exposure sum ?
43
Minimum pKa ?
9
% buried
0
Peptide A name
Zinc finger MYND domain-containing protein 11
Peptide B name
Zinc finger MYND domain-containing protein 11
Peptide A accession
Q15326
Peptide B accession
Q15326
Peptide A residue number
535
Peptide B residue number
535
Ligandability
5hda A 488 C 495
A redox-regulated disulphide may form between two units of Zinc finger MYND domain-containing protein 11 at cysteines 528 and 535 (488 and 495 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
5hda
Structure name
crystal structure of the bs69 coiled coil-mynd domains bound to an ebna2 pxlxp motif
Structure deposition date
2016-01-05
Thiol separation (Å)
10
Half-sphere exposure sum ?
44
Minimum pKa ?
9
% buried
0
Peptide A name
Zinc finger MYND domain-containing protein 11
Peptide B name
Zinc finger MYND domain-containing protein 11
Peptide A accession
Q15326
Peptide B accession
Q15326
Peptide A residue number
528
Peptide B residue number
535
Ligandability
Cysteine 528 of Zinc finger MYND domain-containing protein 11
Cysteine 535 of Zinc finger MYND domain-containing protein 11
5hda C 535 C 558
A redox-regulated disulphide may form within Zinc finger MYND domain-containing protein 11 between cysteines 575 and 598 (535 and 558 respectively in this structure).
Details
Redox score ?
88
PDB code
5hda
Structure name
crystal structure of the bs69 coiled coil-mynd domains bound to an ebna2 pxlxp motif
Structure deposition date
2016-01-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
50
Minimum pKa ?
3
% buried
32
Peptide accession
Q15326
Residue number A
575
Residue number B
598
Peptide name
Zinc finger MYND domain-containing protein 11
Ligandability
Cysteine 575 of Zinc finger MYND domain-containing protein 11
Cysteine 598 of Zinc finger MYND domain-containing protein 11
5hda A 534 A 535
A redox-regulated disulphide may form within Zinc finger MYND domain-containing protein 11 between cysteines 574 and 575 (534 and 535 respectively in this structure).
Details
Redox score ?
83
PDB code
5hda
Structure name
crystal structure of the bs69 coiled coil-mynd domains bound to an ebna2 pxlxp motif
Structure deposition date
2016-01-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
65
Minimum pKa ?
3
% buried
48
Peptide accession
Q15326
Residue number A
574
Residue number B
575
Peptide name
Zinc finger MYND domain-containing protein 11
Ligandability
Cysteine 574 of Zinc finger MYND domain-containing protein 11
Cysteine 575 of Zinc finger MYND domain-containing protein 11
5hda C 523 C 545
A redox-regulated disulphide may form within Zinc finger MYND domain-containing protein 11 between cysteines 563 and 585 (523 and 545 respectively in this structure).
Details
Redox score ?
82
PDB code
5hda
Structure name
crystal structure of the bs69 coiled coil-mynd domains bound to an ebna2 pxlxp motif
Structure deposition date
2016-01-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
6
% buried
27
Peptide accession
Q15326
Residue number A
563
Residue number B
585
Peptide name
Zinc finger MYND domain-containing protein 11
Ligandability
Cysteine 563 of Zinc finger MYND domain-containing protein 11
Cysteine 585 of Zinc finger MYND domain-containing protein 11
5hda C 541 C 545
A redox-regulated disulphide may form within Zinc finger MYND domain-containing protein 11 between cysteines 581 and 585 (541 and 545 respectively in this structure).
Details
Redox score ?
82
PDB code
5hda
Structure name
crystal structure of the bs69 coiled coil-mynd domains bound to an ebna2 pxlxp motif
Structure deposition date
2016-01-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
6
% buried
10
Peptide accession
Q15326
Residue number A
581
Residue number B
585
Peptide name
Zinc finger MYND domain-containing protein 11
Ligandability
Cysteine 581 of Zinc finger MYND domain-containing protein 11
Cysteine 585 of Zinc finger MYND domain-containing protein 11
5hda A 534 A 558
A redox-regulated disulphide may form within Zinc finger MYND domain-containing protein 11 between cysteines 574 and 598 (534 and 558 respectively in this structure).
Details
Redox score ?
81
PDB code
5hda
Structure name
crystal structure of the bs69 coiled coil-mynd domains bound to an ebna2 pxlxp motif
Structure deposition date
2016-01-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
9
% buried
32
Peptide accession
Q15326
Residue number A
574
Residue number B
598
Peptide name
Zinc finger MYND domain-containing protein 11
Ligandability
Cysteine 574 of Zinc finger MYND domain-containing protein 11
Cysteine 598 of Zinc finger MYND domain-containing protein 11
4ns5 A 258 A 277
A redox-regulated disulphide may form within Zinc finger MYND domain-containing protein 11 between cysteines 258 and 277.
Details
Redox score ?
81
PDB code
4ns5
Structure name
crystal structure of human bs69 bromo-zinc finger-pwwp
Structure deposition date
2013-11-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
7
% buried
66
Peptide accession
Q15326
Residue number A
258
Residue number B
277
Peptide name
Zinc finger MYND domain-containing protein 11
Ligandability
Cysteine 258 of Zinc finger MYND domain-containing protein 11
Cysteine 277 of Zinc finger MYND domain-containing protein 11
4ns5 A 258 A 261
A redox-regulated disulphide may form within Zinc finger MYND domain-containing protein 11 between cysteines 258 and 261.
Details
Redox score ?
80
PDB code
4ns5
Structure name
crystal structure of human bs69 bromo-zinc finger-pwwp
Structure deposition date
2013-11-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
7
% buried
nan
Peptide accession
Q15326
Residue number A
258
Residue number B
261
Peptide name
Zinc finger MYND domain-containing protein 11
Ligandability
Cysteine 258 of Zinc finger MYND domain-containing protein 11
Cysteine 261 of Zinc finger MYND domain-containing protein 11
5hda C 526 C 545
A redox-regulated disulphide may form within Zinc finger MYND domain-containing protein 11 between cysteines 566 and 585 (526 and 545 respectively in this structure).
Details
Redox score ?
80
PDB code
5hda
Structure name
crystal structure of the bs69 coiled coil-mynd domains bound to an ebna2 pxlxp motif
Structure deposition date
2016-01-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
6
% buried
8
Peptide accession
Q15326
Residue number A
566
Residue number B
585
Peptide name
Zinc finger MYND domain-containing protein 11
Ligandability
Cysteine 566 of Zinc finger MYND domain-containing protein 11
Cysteine 585 of Zinc finger MYND domain-containing protein 11
5hda A 523 A 526
A redox-regulated disulphide may form within Zinc finger MYND domain-containing protein 11 between cysteines 563 and 566 (523 and 526 respectively in this structure).
Details
Redox score ?
75
PDB code
5hda
Structure name
crystal structure of the bs69 coiled coil-mynd domains bound to an ebna2 pxlxp motif
Structure deposition date
2016-01-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
9
% buried
26
Peptide accession
Q15326
Residue number A
563
Residue number B
566
Peptide name
Zinc finger MYND domain-containing protein 11
Ligandability
Cysteine 563 of Zinc finger MYND domain-containing protein 11
Cysteine 566 of Zinc finger MYND domain-containing protein 11
5hda C 526 C 541
A redox-regulated disulphide may form within Zinc finger MYND domain-containing protein 11 between cysteines 566 and 581 (526 and 541 respectively in this structure).
Details
Redox score ?
74
PDB code
5hda
Structure name
crystal structure of the bs69 coiled coil-mynd domains bound to an ebna2 pxlxp motif
Structure deposition date
2016-01-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
9
% buried
8
Peptide accession
Q15326
Residue number A
566
Residue number B
581
Peptide name
Zinc finger MYND domain-containing protein 11
Ligandability
Cysteine 566 of Zinc finger MYND domain-containing protein 11
Cysteine 581 of Zinc finger MYND domain-containing protein 11
5hda C 523 C 541
A redox-regulated disulphide may form within Zinc finger MYND domain-containing protein 11 between cysteines 563 and 581 (523 and 541 respectively in this structure).
Details
Redox score ?
72
PDB code
5hda
Structure name
crystal structure of the bs69 coiled coil-mynd domains bound to an ebna2 pxlxp motif
Structure deposition date
2016-01-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
9
% buried
26
Peptide accession
Q15326
Residue number A
563
Residue number B
581
Peptide name
Zinc finger MYND domain-containing protein 11
Ligandability
Cysteine 563 of Zinc finger MYND domain-containing protein 11
Cysteine 581 of Zinc finger MYND domain-containing protein 11
4ns5 A 261 A 277
A redox-regulated disulphide may form within Zinc finger MYND domain-containing protein 11 between cysteines 261 and 277. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
56
PDB code
4ns5
Structure name
crystal structure of human bs69 bromo-zinc finger-pwwp
Structure deposition date
2013-11-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
18
% buried
nan
Peptide accession
Q15326
Residue number A
261
Residue number B
277
Peptide name
Zinc finger MYND domain-containing protein 11
Ligandability
Cysteine 261 of Zinc finger MYND domain-containing protein 11
Cysteine 277 of Zinc finger MYND domain-containing protein 11
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