Lysozyme C
Intermolecular
Cysteine 6 and cysteine 6
Cysteine 127 and cysteine 6
Cysteine 127 and cysteine 127
Cysteine 99 and cysteine 99
Cysteine 99 and cysteine 64
Intramolecular
Cysteine 24 and cysteine 146
Cysteine 83 and cysteine 99
Cysteine 95 and cysteine 113
Cysteine 48 and cysteine 134
Cysteine 83 and cysteine 113
More...Cysteine 64 and cysteine 113
Cysteine 64 and cysteine 95
Cysteine 83 and cysteine 95
Cysteine 99 and cysteine 113
Cysteine 95 and cysteine 99
5xuw A 6 B 6
A redox-regulated disulphide may form between two units of Lysozyme C at cysteines 6 and 6.
Details
Redox score ?
70
PDB code
5xuw
Structure name
crystal structure of lysozyme from equus asinus
Structure deposition date
2017-06-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide A name
Lysozyme C
Peptide B name
Lysozyme C
Peptide A accession
P11375
Peptide B accession
P11375
Peptide A residue number
6
Peptide B residue number
6
Ligandability
5xuw A 127 B 6
A redox-regulated disulphide may form between two units of Lysozyme C at cysteines 127 and 6. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
60
PDB code
5xuw
Structure name
crystal structure of lysozyme from equus asinus
Structure deposition date
2017-06-26
Thiol separation (Å)
6
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide A name
Lysozyme C
Peptide B name
Lysozyme C
Peptide A accession
P11375
Peptide B accession
P11375
Peptide A residue number
127
Peptide B residue number
6
Ligandability
Cysteine 127 of Lysozyme C
Cysteine 6 of Lysozyme C
5xuw A 127 B 127
A redox-regulated disulphide may form between two units of Lysozyme C at cysteines 127 and 127. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
5xuw
Structure name
crystal structure of lysozyme from equus asinus
Structure deposition date
2017-06-26
Thiol separation (Å)
8
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide A name
Lysozyme C
Peptide B name
Lysozyme C
Peptide A accession
P11375
Peptide B accession
P11375
Peptide A residue number
127
Peptide B residue number
127
Ligandability
1qsw B 81 C 81
A redox-regulated disulphide may form between two units of Lysozyme C at cysteines 99 and 99 (81 and 81 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
1qsw
Structure name
crystal structure analysis of a human lysozyme mutant w64c c65a
Structure deposition date
1999-06-24
Thiol separation (Å)
7
Half-sphere exposure sum ?
91
Minimum pKa ?
nan
% buried
nan
Peptide A name
Lysozyme C
Peptide B name
Lysozyme C
Peptide A accession
P61626
Peptide B accession
P61626
Peptide A residue number
99
Peptide B residue number
99
Ligandability
1qsw B 81 C 64
A redox-regulated disulphide may form between two units of Lysozyme C at cysteines 99 and 64 (81 and 64 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
1qsw
Structure name
crystal structure analysis of a human lysozyme mutant w64c c65a
Structure deposition date
1999-06-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
86
Minimum pKa ?
nan
% buried
nan
Peptide A name
Lysozyme C
Peptide B name
Lysozyme C
Peptide A accession
P61626
Peptide B accession
P61626
Peptide A residue number
99
Peptide B residue number
64
Ligandability
Cysteine 99 of Lysozyme C
Cysteine 64 of Lysozyme C
Cysteine 64 in protein B could not be asigned to a Uniprot residue.
2hee A 6 A 128
A redox-regulated disulphide may form within Lysozyme C between cysteines 24 and 146 (6 and 128 respectively in this structure).
Details
Redox score ?
88
PDB code
2hee
Structure name
contribution of water molecules in the interior of a protein to the conformational stability
Structure deposition date
1997-09-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
44
Minimum pKa ?
nan
% buried
nan
Peptide accession
P61626
Residue number A
24
Residue number B
146
Peptide name
Lysozyme C
Ligandability
Cysteine 24 of Lysozyme C
Cysteine 146 of Lysozyme C
1c45 A 65 A 81
A redox-regulated disulphide may form within Lysozyme C between cysteines 83 and 99 (65 and 81 respectively in this structure).
Details
Redox score ?
85
PDB code
1c45
Structure name
mutant human lysozyme with foreign n-terminal residues
Structure deposition date
1999-08-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
P61626
Residue number A
83
Residue number B
99
Peptide name
Lysozyme C
Ligandability
Cysteine 83 of Lysozyme C
Cysteine 99 of Lysozyme C
6lfh X 77 X 95
A redox-regulated disulphide may form within Lysozyme C between cysteines 95 and 113 (77 and 95 respectively in this structure).
Details
Redox score ?
84
PDB code
6lfh
Structure name
x-ray crystal structure of chemically synthesized human lysozyme
Structure deposition date
2019-12-02
Thiol separation (Å)
2
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P61626
Residue number A
95
Residue number B
113
Peptide name
Lysozyme C
Ligandability
Cysteine 95 of Lysozyme C
Cysteine 113 of Lysozyme C
1ge0 A 30 A 116
A redox-regulated disulphide may form within Lysozyme C between cysteines 48 and 134 (30 and 116 respectively in this structure).
Details
Redox score ?
82
PDB code
1ge0
Structure name
crystal structure of mutant human lysozyme substituted at left-handed helical positions
Structure deposition date
2000-10-06
Thiol separation (Å)
2
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
P61626
Residue number A
48
Residue number B
134
Peptide name
Lysozyme C
Ligandability
Cysteine 48 of Lysozyme C
Cysteine 134 of Lysozyme C
1gf7 A 65 A 95
A redox-regulated disulphide may form within Lysozyme C between cysteines 83 and 113 (65 and 95 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
57
PDB code
1gf7
Structure name
buried polar mutant human lysozyme
Structure deposition date
2000-11-30
Thiol separation (Å)
6
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P61626
Residue number A
83
Residue number B
113
Peptide name
Lysozyme C
Ligandability
Cysteine 83 of Lysozyme C
Cysteine 113 of Lysozyme C
1qsw B 64 B 95
A redox-regulated disulphide may form within Lysozyme C between cysteines 64 and 113 (64 and 95 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
54
PDB code
1qsw
Structure name
crystal structure analysis of a human lysozyme mutant w64c c65a
Structure deposition date
1999-06-24
Thiol separation (Å)
7
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
P61626
Residue number A
64
Residue number B
113
Peptide name
Lysozyme C
Ligandability
Cysteine 64 of Lysozyme C
Cysteine 113 of Lysozyme C
Cysteine 64 in protein A could not be asigned to a Uniprot residue.
1qsw D 64 D 77
A redox-regulated disulphide may form within Lysozyme C between cysteines 64 and 95 (64 and 77 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
54
PDB code
1qsw
Structure name
crystal structure analysis of a human lysozyme mutant w64c c65a
Structure deposition date
1999-06-24
Thiol separation (Å)
7
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P61626
Residue number A
64
Residue number B
95
Peptide name
Lysozyme C
Ligandability
Cysteine 64 of Lysozyme C
Cysteine 95 of Lysozyme C
Cysteine 64 in protein A could not be asigned to a Uniprot residue.
1lz5 A 65 A 77
A redox-regulated disulphide may form within Lysozyme C between cysteines 83 and 95 (65 and 77 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
1lz5
Structure name
structural and functional analyses of the arg-gly-asp sequence introduced into human lysozyme
Structure deposition date
1993-02-03
Thiol separation (Å)
7
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
P61626
Residue number A
83
Residue number B
95
Peptide name
Lysozyme C
Ligandability
Cysteine 83 of Lysozyme C
Cysteine 95 of Lysozyme C
2mei A 81 A 95
A redox-regulated disulphide may form within Lysozyme C between cysteines 99 and 113 (81 and 95 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
2mei
Structure name
contribution of hydrophobic effect to the conformational stability of human lysozyme
Structure deposition date
1998-05-02
Thiol separation (Å)
9
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P61626
Residue number A
99
Residue number B
113
Peptide name
Lysozyme C
Ligandability
Cysteine 99 of Lysozyme C
Cysteine 113 of Lysozyme C
1ioc A 77 A 81
A redox-regulated disulphide may form within Lysozyme C between cysteines 95 and 99 (77 and 81 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
1ioc
Structure name
crystal structure of mutant human lysozyme, eaea-i56t
Structure deposition date
2001-02-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P61626
Residue number A
95
Residue number B
99
Peptide name
Lysozyme C
Ligandability
Cysteine 95 of Lysozyme C
Cysteine 99 of Lysozyme C
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