Protein fem-1 homolog C
Intermolecular
Cysteine 64 and cysteine 64
Cysteine 357 and cysteine 357
Cysteine 205 and cysteine 205
Intramolecular
Cysteine 157 and cysteine 189
Cysteine 124 and cysteine 152
Cysteine 124 and cysteine 157
6xkc A 64 E 64
A redox-regulated disulphide may form between two units of Protein fem-1 homolog C at cysteines 64 and 64. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
60
PDB code
6xkc
Structure name
crystal structure of e3 ligase
Structure deposition date
2020-06-26
Thiol separation (Å)
7
Half-sphere exposure sum ?
71
Minimum pKa ?
9
% buried
60
Peptide A name
Protein fem-1 homolog C
Peptide B name
Protein fem-1 homolog C
Peptide A accession
Q96JP0
Peptide B accession
Q96JP0
Peptide A residue number
64
Peptide B residue number
64
Ligandability
7jya B 357 C 357
A redox-regulated disulphide may form between two units of Protein fem-1 homolog C at cysteines 357 and 357. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
7jya
Structure name
crystal structure of e3 ligase in complex with peptide
Structure deposition date
2020-08-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide A name
Protein fem-1 homolog C
Peptide B name
Protein fem-1 homolog C
Peptide A accession
Q96JP0
Peptide B accession
Q96JP0
Peptide A residue number
357
Peptide B residue number
357
Ligandability
6xkc B 205 E 205
A redox-regulated disulphide may form between two units of Protein fem-1 homolog C at cysteines 205 and 205. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
6xkc
Structure name
crystal structure of e3 ligase
Structure deposition date
2020-06-26
Thiol separation (Å)
10
Half-sphere exposure sum ?
52
Minimum pKa ?
9
% buried
20
Peptide A name
Protein fem-1 homolog C
Peptide B name
Protein fem-1 homolog C
Peptide A accession
Q96JP0
Peptide B accession
Q96JP0
Peptide A residue number
205
Peptide B residue number
205
Ligandability
6lf0 B 157 B 189
A redox-regulated disulphide may form within Protein fem-1 homolog C between cysteines 157 and 189.
Details
Redox score ?
65
PDB code
6lf0
Structure name
structure of fem1c
Structure deposition date
2019-11-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
88
Minimum pKa ?
10
% buried
96
Peptide accession
Q96JP0
Residue number A
157
Residue number B
189
Peptide name
Protein fem-1 homolog C
Ligandability
Cysteine 157 of Protein fem-1 homolog C
Cysteine 189 of Protein fem-1 homolog C
6len B 124 B 152
A redox-regulated disulphide may form within Protein fem-1 homolog C between cysteines 124 and 152.
Details
Redox score ?
63
PDB code
6len
Structure name
structure of ns11 bound fem1c
Structure deposition date
2019-11-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
97
Minimum pKa ?
8
% buried
100
Peptide accession
Q96JP0
Residue number A
124
Residue number B
152
Peptide name
Protein fem-1 homolog C
Ligandability
Cysteine 124 of Protein fem-1 homolog C
Cysteine 152 of Protein fem-1 homolog C
6lf0 B 124 B 157
A redox-regulated disulphide may form within Protein fem-1 homolog C between cysteines 124 and 157. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
17
PDB code
6lf0
Structure name
structure of fem1c
Structure deposition date
2019-11-27
Thiol separation (Å)
10
Half-sphere exposure sum ?
91
Minimum pKa ?
17
% buried
100
Peptide accession
Q96JP0
Residue number A
124
Residue number B
157
Peptide name
Protein fem-1 homolog C
Ligandability
Cysteine 124 of Protein fem-1 homolog C
Cysteine 157 of Protein fem-1 homolog C
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