Protein inturned
Intermolecular
Cysteine 838 and cysteine 365 of Fuzzy planar cell polarity protein
Cysteine 838 and cysteine 365 of Protein fuzzy homolog
Intramolecular
Cysteine 542 and cysteine 602
Cysteine 838 and cysteine 839
Cysteine 885 and cysteine 920
Cysteine 839 and cysteine 920
Cysteine 838 and cysteine 920
7q3e B 838 C 365
A redox-regulated disulphide may form between cysteine 838 of Protein inturned and cysteine 365 of Fuzzy planar cell polarity protein. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
7q3e
Structure name
structure of the mouse cplane-rsg1 complex
Structure deposition date
2021-10-27
Thiol separation (Å)
7
Half-sphere exposure sum ?
82
Minimum pKa ?
12
% buried
100
Peptide A name
Protein inturned
Peptide B name
Fuzzy planar cell polarity protein
Peptide A accession
Q059U7
Peptide B accession
E9QL29
Peptide A residue number
838
Peptide B residue number
365
Ligandability
Cysteine 838 of Protein inturned
Cysteine 365 of Fuzzy planar cell polarity protein
7q3d B 838 C 365
A redox-regulated disulphide may form between cysteine 838 of Protein inturned and cysteine 365 of Protein fuzzy homolog. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
29
PDB code
7q3d
Structure name
structure of the human cplane complex
Structure deposition date
2021-10-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
82
Minimum pKa ?
12
% buried
96
Peptide A name
Protein inturned
Peptide B name
Protein fuzzy homolog
Peptide A accession
Q9ULD6
Peptide B accession
Q9BT04
Peptide A residue number
838
Peptide B residue number
365
Ligandability
Cysteine 838 of Protein inturned
Cysteine 365 of Protein fuzzy homolog
7q3d B 542 B 602
A redox-regulated disulphide may form within Protein inturned between cysteines 542 and 602.
Details
Redox score ?
60
PDB code
7q3d
Structure name
structure of the human cplane complex
Structure deposition date
2021-10-27
Thiol separation (Å)
5
Half-sphere exposure sum ?
83
Minimum pKa ?
9
% buried
100
Peptide accession
Q9ULD6
Residue number A
542
Residue number B
602
Peptide name
Protein inturned
Ligandability
Cysteine 542 of Protein inturned
Cysteine 602 of Protein inturned
7q3e B 838 B 839
A redox-regulated disulphide may form within Protein inturned between cysteines 838 and 839. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
7q3e
Structure name
structure of the mouse cplane-rsg1 complex
Structure deposition date
2021-10-27
Thiol separation (Å)
6
Half-sphere exposure sum ?
81
Minimum pKa ?
12
% buried
100
Peptide accession
Q059U7
Residue number A
838
Residue number B
839
Peptide name
Protein inturned
Ligandability
Cysteine 838 of Protein inturned
Cysteine 839 of Protein inturned
7q3e B 885 B 920
A redox-regulated disulphide may form within Protein inturned between cysteines 885 and 920. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
36
PDB code
7q3e
Structure name
structure of the mouse cplane-rsg1 complex
Structure deposition date
2021-10-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
72
Minimum pKa ?
11
% buried
72
Peptide accession
Q059U7
Residue number A
885
Residue number B
920
Peptide name
Protein inturned
Ligandability
Cysteine 885 of Protein inturned
Cysteine 920 of Protein inturned
7q3d B 839 B 920
A redox-regulated disulphide may form within Protein inturned between cysteines 839 and 920. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
7q3d
Structure name
structure of the human cplane complex
Structure deposition date
2021-10-27
Thiol separation (Å)
8
Half-sphere exposure sum ?
87
Minimum pKa ?
13
% buried
100
Peptide accession
Q9ULD6
Residue number A
839
Residue number B
920
Peptide name
Protein inturned
Ligandability
Cysteine 839 of Protein inturned
Cysteine 920 of Protein inturned
7q3d B 838 B 920
A redox-regulated disulphide may form within Protein inturned between cysteines 838 and 920. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
32
PDB code
7q3d
Structure name
structure of the human cplane complex
Structure deposition date
2021-10-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
80
Minimum pKa ?
12
% buried
96
Peptide accession
Q9ULD6
Residue number A
838
Residue number B
920
Peptide name
Protein inturned
Ligandability
Cysteine 838 of Protein inturned
Cysteine 920 of Protein inturned
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