Chromodomain-helicase-DNA-binding protein 4
Intramolecular
Cysteine 464 and cysteine 493
Cysteine 373 and cysteine 376
Cysteine 467 and cysteine 493
Cysteine 373 and cysteine 396
Cysteine 464 and cysteine 467
Cysteine 385 and cysteine 414
Cysteine 385 and cysteine 388
Cysteine 464 and cysteine 490
Cysteine 385 and cysteine 411
Cysteine 467 and cysteine 490
More...Cysteine 452 and cysteine 455
Cysteine 452 and cysteine 475
Cysteine 388 and cysteine 414
Cysteine 411 and cysteine 414
Cysteine 490 and cysteine 493
Cysteine 376 and cysteine 396
Cysteine 388 and cysteine 411
Cysteine 455 and cysteine 475
Cysteine 467 and cysteine 495
Cysteine 463 and cysteine 464
Cysteine 452 and cysteine 493
Cysteine 455 and cysteine 495
Cysteine 463 and cysteine 493
Cysteine 1018 and cysteine 1019
Cysteine 475 and cysteine 493
Cysteine 475 and cysteine 495
Cysteine 452 and cysteine 463
Cysteine 493 and cysteine 495
Cysteine 490 and cysteine 495
Cysteine 463 and cysteine 490
Cysteine 452 and cysteine 495
Cysteine 452 and cysteine 464
Cysteine 464 and cysteine 495
Cysteine 464 and cysteine 475
Cysteine 463 and cysteine 467
6q3m C 464 C 493
A redox-regulated disulphide may form within Chromodomain-helicase-DNA-binding protein 4 between cysteines 464 and 493.
Details
Redox score ?
90
PDB code
6q3m
Structure name
structure of chd4 phd2 - tandem chromodomains
Structure deposition date
2018-12-04
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
5
% buried
13
Peptide accession
Q14839
Residue number A
464
Residue number B
493
Peptide name
Chromodomain-helicase-DNA-binding protein 4
Ligandability
Cysteine 464 of Chromodomain-helicase-DNA-binding protein 4
Cysteine 493 of Chromodomain-helicase-DNA-binding protein 4
2l5u A 14 A 17
A redox-regulated disulphide may form within Chromodomain-helicase-DNA-binding protein 4 between cysteines 373 and 376 (14 and 17 respectively in this structure).
Details
Redox score ?
89
PDB code
2l5u
Structure name
structure of the first phd finger (phd1) from chd4 (mi2b)
Structure deposition date
2010-11-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
44
Minimum pKa ?
5
% buried
0
Peptide accession
Q14839
Residue number A
373
Residue number B
376
Peptide name
Chromodomain-helicase-DNA-binding protein 4
Ligandability
Cysteine 373 of Chromodomain-helicase-DNA-binding protein 4
Cysteine 376 of Chromodomain-helicase-DNA-binding protein 4
6q3m A 467 A 493
A redox-regulated disulphide may form within Chromodomain-helicase-DNA-binding protein 4 between cysteines 467 and 493.
Details
Redox score ?
89
PDB code
6q3m
Structure name
structure of chd4 phd2 - tandem chromodomains
Structure deposition date
2018-12-04
Thiol separation (Å)
4
Half-sphere exposure sum ?
42
Minimum pKa ?
5
% buried
17
Peptide accession
Q14839
Residue number A
467
Residue number B
493
Peptide name
Chromodomain-helicase-DNA-binding protein 4
Ligandability
Cysteine 467 of Chromodomain-helicase-DNA-binding protein 4
Cysteine 493 of Chromodomain-helicase-DNA-binding protein 4
2l5u A 14 A 37
A redox-regulated disulphide may form within Chromodomain-helicase-DNA-binding protein 4 between cysteines 373 and 396 (14 and 37 respectively in this structure).
Details
Redox score ?
88
PDB code
2l5u
Structure name
structure of the first phd finger (phd1) from chd4 (mi2b)
Structure deposition date
2010-11-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
5
% buried
1
Peptide accession
Q14839
Residue number A
373
Residue number B
396
Peptide name
Chromodomain-helicase-DNA-binding protein 4
Ligandability
Cysteine 373 of Chromodomain-helicase-DNA-binding protein 4
Cysteine 396 of Chromodomain-helicase-DNA-binding protein 4
6q3m A 464 A 467
A redox-regulated disulphide may form within Chromodomain-helicase-DNA-binding protein 4 between cysteines 464 and 467.
Details
Redox score ?
85
PDB code
6q3m
Structure name
structure of chd4 phd2 - tandem chromodomains
Structure deposition date
2018-12-04
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
5
% buried
24
Peptide accession
Q14839
Residue number A
464
Residue number B
467
Peptide name
Chromodomain-helicase-DNA-binding protein 4
Ligandability
Cysteine 464 of Chromodomain-helicase-DNA-binding protein 4
Cysteine 467 of Chromodomain-helicase-DNA-binding protein 4
2l5u A 26 A 55
A redox-regulated disulphide may form within Chromodomain-helicase-DNA-binding protein 4 between cysteines 385 and 414 (26 and 55 respectively in this structure).
Details
Redox score ?
85
PDB code
2l5u
Structure name
structure of the first phd finger (phd1) from chd4 (mi2b)
Structure deposition date
2010-11-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
5
% buried
16
Peptide accession
Q14839
Residue number A
385
Residue number B
414
Peptide name
Chromodomain-helicase-DNA-binding protein 4
Ligandability
Cysteine 385 of Chromodomain-helicase-DNA-binding protein 4
Cysteine 414 of Chromodomain-helicase-DNA-binding protein 4
2l5u A 26 A 29
A redox-regulated disulphide may form within Chromodomain-helicase-DNA-binding protein 4 between cysteines 385 and 388 (26 and 29 respectively in this structure).
Details
Redox score ?
82
PDB code
2l5u
Structure name
structure of the first phd finger (phd1) from chd4 (mi2b)
Structure deposition date
2010-11-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
5
% buried
22
Peptide accession
Q14839
Residue number A
385
Residue number B
388
Peptide name
Chromodomain-helicase-DNA-binding protein 4
Ligandability
Cysteine 385 of Chromodomain-helicase-DNA-binding protein 4
Cysteine 388 of Chromodomain-helicase-DNA-binding protein 4
6q3m A 464 A 490
A redox-regulated disulphide may form within Chromodomain-helicase-DNA-binding protein 4 between cysteines 464 and 490.
Details
Redox score ?
82
PDB code
6q3m
Structure name
structure of chd4 phd2 - tandem chromodomains
Structure deposition date
2018-12-04
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
7
% buried
31
Peptide accession
Q14839
Residue number A
464
Residue number B
490
Peptide name
Chromodomain-helicase-DNA-binding protein 4
Ligandability
Cysteine 464 of Chromodomain-helicase-DNA-binding protein 4
Cysteine 490 of Chromodomain-helicase-DNA-binding protein 4
2l5u A 26 A 52
A redox-regulated disulphide may form within Chromodomain-helicase-DNA-binding protein 4 between cysteines 385 and 411 (26 and 52 respectively in this structure).
Details
Redox score ?
82
PDB code
2l5u
Structure name
structure of the first phd finger (phd1) from chd4 (mi2b)
Structure deposition date
2010-11-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
5
% buried
28
Peptide accession
Q14839
Residue number A
385
Residue number B
411
Peptide name
Chromodomain-helicase-DNA-binding protein 4
Ligandability
Cysteine 385 of Chromodomain-helicase-DNA-binding protein 4
Cysteine 411 of Chromodomain-helicase-DNA-binding protein 4
6q3m C 467 C 490
A redox-regulated disulphide may form within Chromodomain-helicase-DNA-binding protein 4 between cysteines 467 and 490.
Details
Redox score ?
82
PDB code
6q3m
Structure name
structure of chd4 phd2 - tandem chromodomains
Structure deposition date
2018-12-04
Thiol separation (Å)
3
Half-sphere exposure sum ?
52
Minimum pKa ?
7
% buried
38
Peptide accession
Q14839
Residue number A
467
Residue number B
490
Peptide name
Chromodomain-helicase-DNA-binding protein 4
Ligandability
Cysteine 467 of Chromodomain-helicase-DNA-binding protein 4
Cysteine 490 of Chromodomain-helicase-DNA-binding protein 4
6q3m D 452 D 455
A redox-regulated disulphide may form within Chromodomain-helicase-DNA-binding protein 4 between cysteines 452 and 455.
Details
Redox score ?
82
PDB code
6q3m
Structure name
structure of chd4 phd2 - tandem chromodomains
Structure deposition date
2018-12-04
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
6
% buried
15
Peptide accession
Q14839
Residue number A
452
Residue number B
455
Peptide name
Chromodomain-helicase-DNA-binding protein 4
Ligandability
Cysteine 452 of Chromodomain-helicase-DNA-binding protein 4
Cysteine 455 of Chromodomain-helicase-DNA-binding protein 4
6q3m A 452 A 475
A redox-regulated disulphide may form within Chromodomain-helicase-DNA-binding protein 4 between cysteines 452 and 475.
Details
Redox score ?
81
PDB code
6q3m
Structure name
structure of chd4 phd2 - tandem chromodomains
Structure deposition date
2018-12-04
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
6
% buried
28
Peptide accession
Q14839
Residue number A
452
Residue number B
475
Peptide name
Chromodomain-helicase-DNA-binding protein 4
Ligandability
Cysteine 452 of Chromodomain-helicase-DNA-binding protein 4
Cysteine 475 of Chromodomain-helicase-DNA-binding protein 4
2l5u A 29 A 55
A redox-regulated disulphide may form within Chromodomain-helicase-DNA-binding protein 4 between cysteines 388 and 414 (29 and 55 respectively in this structure).
Details
Redox score ?
81
PDB code
2l5u
Structure name
structure of the first phd finger (phd1) from chd4 (mi2b)
Structure deposition date
2010-11-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
43
Minimum pKa ?
9
% buried
11
Peptide accession
Q14839
Residue number A
388
Residue number B
414
Peptide name
Chromodomain-helicase-DNA-binding protein 4
Ligandability
Cysteine 388 of Chromodomain-helicase-DNA-binding protein 4
Cysteine 414 of Chromodomain-helicase-DNA-binding protein 4
2l5u A 52 A 55
A redox-regulated disulphide may form within Chromodomain-helicase-DNA-binding protein 4 between cysteines 411 and 414 (52 and 55 respectively in this structure).
Details
Redox score ?
80
PDB code
2l5u
Structure name
structure of the first phd finger (phd1) from chd4 (mi2b)
Structure deposition date
2010-11-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
9
% buried
17
Peptide accession
Q14839
Residue number A
411
Residue number B
414
Peptide name
Chromodomain-helicase-DNA-binding protein 4
Ligandability
Cysteine 411 of Chromodomain-helicase-DNA-binding protein 4
Cysteine 414 of Chromodomain-helicase-DNA-binding protein 4
6q3m A 490 A 493
A redox-regulated disulphide may form within Chromodomain-helicase-DNA-binding protein 4 between cysteines 490 and 493.
Details
Redox score ?
78
PDB code
6q3m
Structure name
structure of chd4 phd2 - tandem chromodomains
Structure deposition date
2018-12-04
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
9
% buried
24
Peptide accession
Q14839
Residue number A
490
Residue number B
493
Peptide name
Chromodomain-helicase-DNA-binding protein 4
Ligandability
Cysteine 490 of Chromodomain-helicase-DNA-binding protein 4
Cysteine 493 of Chromodomain-helicase-DNA-binding protein 4
2l5u A 17 A 37
A redox-regulated disulphide may form within Chromodomain-helicase-DNA-binding protein 4 between cysteines 376 and 396 (17 and 37 respectively in this structure).
Details
Redox score ?
78
PDB code
2l5u
Structure name
structure of the first phd finger (phd1) from chd4 (mi2b)
Structure deposition date
2010-11-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
40
Minimum pKa ?
10
% buried
1
Peptide accession
Q14839
Residue number A
376
Residue number B
396
Peptide name
Chromodomain-helicase-DNA-binding protein 4
Ligandability
Cysteine 376 of Chromodomain-helicase-DNA-binding protein 4
Cysteine 396 of Chromodomain-helicase-DNA-binding protein 4
2l5u A 29 A 52
A redox-regulated disulphide may form within Chromodomain-helicase-DNA-binding protein 4 between cysteines 388 and 411 (29 and 52 respectively in this structure).
Details
Redox score ?
78
PDB code
2l5u
Structure name
structure of the first phd finger (phd1) from chd4 (mi2b)
Structure deposition date
2010-11-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
9
% buried
23
Peptide accession
Q14839
Residue number A
388
Residue number B
411
Peptide name
Chromodomain-helicase-DNA-binding protein 4
Ligandability
Cysteine 388 of Chromodomain-helicase-DNA-binding protein 4
Cysteine 411 of Chromodomain-helicase-DNA-binding protein 4
6q3m A 455 A 475
A redox-regulated disulphide may form within Chromodomain-helicase-DNA-binding protein 4 between cysteines 455 and 475.
Details
Redox score ?
76
PDB code
6q3m
Structure name
structure of chd4 phd2 - tandem chromodomains
Structure deposition date
2018-12-04
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
9
% buried
10
Peptide accession
Q14839
Residue number A
455
Residue number B
475
Peptide name
Chromodomain-helicase-DNA-binding protein 4
Ligandability
Cysteine 455 of Chromodomain-helicase-DNA-binding protein 4
Cysteine 475 of Chromodomain-helicase-DNA-binding protein 4
1mm3 A 27 A 55
A redox-regulated disulphide may form within Chromodomain-helicase-DNA-binding protein 4 between cysteines 467 and 495 (27 and 55 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
59
PDB code
1mm3
Structure name
solution structure of the 2nd phd domain from mi2b with c-terminal loop replaced by corresponding loop from wstf
Structure deposition date
2002-09-02
Thiol separation (Å)
7
Half-sphere exposure sum ?
38
Minimum pKa ?
9
% buried
4
Peptide accession
Q14839
Residue number A
467
Residue number B
495
Peptide name
Chromodomain-helicase-DNA-binding protein 4
Ligandability
Cysteine 467 of Chromodomain-helicase-DNA-binding protein 4
Cysteine 495 of Chromodomain-helicase-DNA-binding protein 4
6q3m B 463 B 464
A redox-regulated disulphide may form within Chromodomain-helicase-DNA-binding protein 4 between cysteines 463 and 464. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
53
PDB code
6q3m
Structure name
structure of chd4 phd2 - tandem chromodomains
Structure deposition date
2018-12-04
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
5
% buried
34
Peptide accession
Q14839
Residue number A
463
Residue number B
464
Peptide name
Chromodomain-helicase-DNA-binding protein 4
Ligandability
Cysteine 463 of Chromodomain-helicase-DNA-binding protein 4
Cysteine 464 of Chromodomain-helicase-DNA-binding protein 4
1mm3 A 12 A 53
A redox-regulated disulphide may form within Chromodomain-helicase-DNA-binding protein 4 between cysteines 452 and 493 (12 and 53 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
53
PDB code
1mm3
Structure name
solution structure of the 2nd phd domain from mi2b with c-terminal loop replaced by corresponding loop from wstf
Structure deposition date
2002-09-02
Thiol separation (Å)
9
Half-sphere exposure sum ?
61
Minimum pKa ?
6
% buried
14
Peptide accession
Q14839
Residue number A
452
Residue number B
493
Peptide name
Chromodomain-helicase-DNA-binding protein 4
Ligandability
Cysteine 452 of Chromodomain-helicase-DNA-binding protein 4
Cysteine 493 of Chromodomain-helicase-DNA-binding protein 4
1mm3 A 15 A 55
A redox-regulated disulphide may form within Chromodomain-helicase-DNA-binding protein 4 between cysteines 455 and 495 (15 and 55 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
1mm3
Structure name
solution structure of the 2nd phd domain from mi2b with c-terminal loop replaced by corresponding loop from wstf
Structure deposition date
2002-09-02
Thiol separation (Å)
8
Half-sphere exposure sum ?
34
Minimum pKa ?
9
% buried
0
Peptide accession
Q14839
Residue number A
455
Residue number B
495
Peptide name
Chromodomain-helicase-DNA-binding protein 4
Ligandability
Cysteine 455 of Chromodomain-helicase-DNA-binding protein 4
Cysteine 495 of Chromodomain-helicase-DNA-binding protein 4
1mm3 A 23 A 53
A redox-regulated disulphide may form within Chromodomain-helicase-DNA-binding protein 4 between cysteines 463 and 493 (23 and 53 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
1mm3
Structure name
solution structure of the 2nd phd domain from mi2b with c-terminal loop replaced by corresponding loop from wstf
Structure deposition date
2002-09-02
Thiol separation (Å)
9
Half-sphere exposure sum ?
60
Minimum pKa ?
6
% buried
16
Peptide accession
Q14839
Residue number A
463
Residue number B
493
Peptide name
Chromodomain-helicase-DNA-binding protein 4
Ligandability
Cysteine 463 of Chromodomain-helicase-DNA-binding protein 4
Cysteine 493 of Chromodomain-helicase-DNA-binding protein 4
6ryr W 1018 W 1019
A redox-regulated disulphide may form within Chromodomain-helicase-DNA-binding protein 4 between cysteines 1018 and 1019. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
6ryr
Structure name
nucleosome-chd4 complex structure (single chd4 copy)
Structure deposition date
2019-06-11
Thiol separation (Å)
6
Half-sphere exposure sum ?
86
Minimum pKa ?
12
% buried
91
Peptide accession
Q14839
Residue number A
1018
Residue number B
1019
Peptide name
Chromodomain-helicase-DNA-binding protein 4
Ligandability
Cysteine 1018 of Chromodomain-helicase-DNA-binding protein 4
Cysteine 1019 of Chromodomain-helicase-DNA-binding protein 4
1mm3 A 35 A 53
A redox-regulated disulphide may form within Chromodomain-helicase-DNA-binding protein 4 between cysteines 475 and 493 (35 and 53 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
1mm3
Structure name
solution structure of the 2nd phd domain from mi2b with c-terminal loop replaced by corresponding loop from wstf
Structure deposition date
2002-09-02
Thiol separation (Å)
10
Half-sphere exposure sum ?
61
Minimum pKa ?
6
% buried
14
Peptide accession
Q14839
Residue number A
475
Residue number B
493
Peptide name
Chromodomain-helicase-DNA-binding protein 4
Ligandability
Cysteine 475 of Chromodomain-helicase-DNA-binding protein 4
Cysteine 493 of Chromodomain-helicase-DNA-binding protein 4
1mm3 A 35 A 55
A redox-regulated disulphide may form within Chromodomain-helicase-DNA-binding protein 4 between cysteines 475 and 495 (35 and 55 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
1mm3
Structure name
solution structure of the 2nd phd domain from mi2b with c-terminal loop replaced by corresponding loop from wstf
Structure deposition date
2002-09-02
Thiol separation (Å)
9
Half-sphere exposure sum ?
45
Minimum pKa ?
9
% buried
5
Peptide accession
Q14839
Residue number A
475
Residue number B
495
Peptide name
Chromodomain-helicase-DNA-binding protein 4
Ligandability
Cysteine 475 of Chromodomain-helicase-DNA-binding protein 4
Cysteine 495 of Chromodomain-helicase-DNA-binding protein 4
6q3m C 452 C 463
A redox-regulated disulphide may form within Chromodomain-helicase-DNA-binding protein 4 between cysteines 452 and 463. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
6q3m
Structure name
structure of chd4 phd2 - tandem chromodomains
Structure deposition date
2018-12-04
Thiol separation (Å)
10
Half-sphere exposure sum ?
66
Minimum pKa ?
6
% buried
44
Peptide accession
Q14839
Residue number A
452
Residue number B
463
Peptide name
Chromodomain-helicase-DNA-binding protein 4
Ligandability
Cysteine 452 of Chromodomain-helicase-DNA-binding protein 4
Cysteine 463 of Chromodomain-helicase-DNA-binding protein 4
6q3m A 493 A 495
A redox-regulated disulphide may form within Chromodomain-helicase-DNA-binding protein 4 between cysteines 493 and 495. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
6q3m
Structure name
structure of chd4 phd2 - tandem chromodomains
Structure deposition date
2018-12-04
Thiol separation (Å)
10
Half-sphere exposure sum ?
38
Minimum pKa ?
9
% buried
17
Peptide accession
Q14839
Residue number A
493
Residue number B
495
Peptide name
Chromodomain-helicase-DNA-binding protein 4
Ligandability
Cysteine 493 of Chromodomain-helicase-DNA-binding protein 4
Cysteine 495 of Chromodomain-helicase-DNA-binding protein 4
6q3m D 490 D 495
A redox-regulated disulphide may form within Chromodomain-helicase-DNA-binding protein 4 between cysteines 490 and 495. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
6q3m
Structure name
structure of chd4 phd2 - tandem chromodomains
Structure deposition date
2018-12-04
Thiol separation (Å)
9
Half-sphere exposure sum ?
48
Minimum pKa ?
10
% buried
31
Peptide accession
Q14839
Residue number A
490
Residue number B
495
Peptide name
Chromodomain-helicase-DNA-binding protein 4
Ligandability
Cysteine 490 of Chromodomain-helicase-DNA-binding protein 4
Cysteine 495 of Chromodomain-helicase-DNA-binding protein 4
1mm3 A 23 A 50
A redox-regulated disulphide may form within Chromodomain-helicase-DNA-binding protein 4 between cysteines 463 and 490 (23 and 50 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
1mm3
Structure name
solution structure of the 2nd phd domain from mi2b with c-terminal loop replaced by corresponding loop from wstf
Structure deposition date
2002-09-02
Thiol separation (Å)
10
Half-sphere exposure sum ?
62
Minimum pKa ?
9
% buried
16
Peptide accession
Q14839
Residue number A
463
Residue number B
490
Peptide name
Chromodomain-helicase-DNA-binding protein 4
Ligandability
Cysteine 463 of Chromodomain-helicase-DNA-binding protein 4
Cysteine 490 of Chromodomain-helicase-DNA-binding protein 4
1mm3 A 12 A 55
A redox-regulated disulphide may form within Chromodomain-helicase-DNA-binding protein 4 between cysteines 452 and 495 (12 and 55 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
1mm3
Structure name
solution structure of the 2nd phd domain from mi2b with c-terminal loop replaced by corresponding loop from wstf
Structure deposition date
2002-09-02
Thiol separation (Å)
9
Half-sphere exposure sum ?
45
Minimum pKa ?
9
% buried
6
Peptide accession
Q14839
Residue number A
452
Residue number B
495
Peptide name
Chromodomain-helicase-DNA-binding protein 4
Ligandability
Cysteine 452 of Chromodomain-helicase-DNA-binding protein 4
Cysteine 495 of Chromodomain-helicase-DNA-binding protein 4
1mm3 A 12 A 24
A redox-regulated disulphide may form within Chromodomain-helicase-DNA-binding protein 4 between cysteines 452 and 464 (12 and 24 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
1mm3
Structure name
solution structure of the 2nd phd domain from mi2b with c-terminal loop replaced by corresponding loop from wstf
Structure deposition date
2002-09-02
Thiol separation (Å)
10
Half-sphere exposure sum ?
55
Minimum pKa ?
9
% buried
18
Peptide accession
Q14839
Residue number A
452
Residue number B
464
Peptide name
Chromodomain-helicase-DNA-binding protein 4
Ligandability
Cysteine 452 of Chromodomain-helicase-DNA-binding protein 4
Cysteine 464 of Chromodomain-helicase-DNA-binding protein 4
1mm3 A 24 A 55
A redox-regulated disulphide may form within Chromodomain-helicase-DNA-binding protein 4 between cysteines 464 and 495 (24 and 55 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
1mm3
Structure name
solution structure of the 2nd phd domain from mi2b with c-terminal loop replaced by corresponding loop from wstf
Structure deposition date
2002-09-02
Thiol separation (Å)
10
Half-sphere exposure sum ?
42
Minimum pKa ?
9
% buried
13
Peptide accession
Q14839
Residue number A
464
Residue number B
495
Peptide name
Chromodomain-helicase-DNA-binding protein 4
Ligandability
Cysteine 464 of Chromodomain-helicase-DNA-binding protein 4
Cysteine 495 of Chromodomain-helicase-DNA-binding protein 4
1mm3 A 24 A 35
A redox-regulated disulphide may form within Chromodomain-helicase-DNA-binding protein 4 between cysteines 464 and 475 (24 and 35 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
1mm3
Structure name
solution structure of the 2nd phd domain from mi2b with c-terminal loop replaced by corresponding loop from wstf
Structure deposition date
2002-09-02
Thiol separation (Å)
10
Half-sphere exposure sum ?
55
Minimum pKa ?
9
% buried
17
Peptide accession
Q14839
Residue number A
464
Residue number B
475
Peptide name
Chromodomain-helicase-DNA-binding protein 4
Ligandability
Cysteine 464 of Chromodomain-helicase-DNA-binding protein 4
Cysteine 475 of Chromodomain-helicase-DNA-binding protein 4
6q3m D 463 D 467
A redox-regulated disulphide may form within Chromodomain-helicase-DNA-binding protein 4 between cysteines 463 and 467. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
6q3m
Structure name
structure of chd4 phd2 - tandem chromodomains
Structure deposition date
2018-12-04
Thiol separation (Å)
10
Half-sphere exposure sum ?
57
Minimum pKa ?
7
% buried
38
Peptide accession
Q14839
Residue number A
463
Residue number B
467
Peptide name
Chromodomain-helicase-DNA-binding protein 4
Ligandability
Cysteine 463 of Chromodomain-helicase-DNA-binding protein 4
Cysteine 467 of Chromodomain-helicase-DNA-binding protein 4
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