Beta-2-microglobulin
Intermolecular
Cysteine 45 and cysteine 100
Cysteine 45 and cysteine 45
Cysteine 100 and cysteine 100
Intramolecular
Cysteine 45 and cysteine 100
Cysteine 45 and cysteine 91
6gk3 E 25 F 80
A redox-regulated disulphide may form between two units of Beta-2-microglobulin at cysteines 45 and 100 (25 and 80 respectively in this structure).
Details
Redox score ?
63
PDB code
6gk3
Structure name
two protofilament beta-2-microglobulin amyloid fibril
Structure deposition date
2018-05-18
Thiol separation (Å)
5
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide A name
Beta-2-microglobulin
Peptide B name
Beta-2-microglobulin
Peptide A accession
P61769
Peptide B accession
P61769
Peptide A residue number
45
Peptide B residue number
100
Ligandability
Cysteine 45 of Beta-2-microglobulin
Cysteine 100 of Beta-2-microglobulin
2e8d B 28 D 72
A redox-regulated disulphide may form between two units of Beta-2-microglobulin at cysteines 45 and 45 (28 and 72 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
2e8d
Structure name
3d structure of amyloid protofilaments of beta2-microglobulin fragment probed by solid-state nmr
Structure deposition date
2007-01-19
Thiol separation (Å)
9
Half-sphere exposure sum ?
45
Minimum pKa ?
9
% buried
10
Peptide A name
Beta-2-microglobulin
Peptide B name
Beta-2-microglobulin
Peptide A accession
P61769
Peptide B accession
P61769
Peptide A residue number
45
Peptide B residue number
45
Ligandability
Cysteine 45 of Beta-2-microglobulin
Cysteine 45 of Beta-2-microglobulin
6gk3 F 80 H 80
A redox-regulated disulphide may form between two units of Beta-2-microglobulin at cysteines 100 and 100 (80 and 80 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
6gk3
Structure name
two protofilament beta-2-microglobulin amyloid fibril
Structure deposition date
2018-05-18
Thiol separation (Å)
10
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide A name
Beta-2-microglobulin
Peptide B name
Beta-2-microglobulin
Peptide A accession
P61769
Peptide B accession
P61769
Peptide A residue number
100
Peptide B residue number
100
Ligandability
2av1 E 25 E 80
A redox-regulated disulphide may form within Beta-2-microglobulin between cysteines 45 and 100 (25 and 80 respectively in this structure).
Details
Redox score ?
80
PDB code
2av1
Structure name
crystal structure of htlv-1 tax peptide bound to human class i mhc hla-a2 with the e63q and k66a mutations in the heavy chain
Structure deposition date
2005-08-29
Thiol separation (Å)
2
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
nan
Peptide accession
P61770
Residue number A
45
Residue number B
100
Peptide name
Beta-2-microglobulin
Ligandability
Cysteine 45 of Beta-2-microglobulin
Cysteine 100 of Beta-2-microglobulin
2f53 B 25 B 91
A redox-regulated disulphide may form within Beta-2-microglobulin between cysteines 45 and 91 (25 and 91 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
2f53
Structure name
directed evolution of human t-cell receptor cdr2 residues by phage display dramatically enhances affinity for cognate peptide-mhc without apparent cross-reactivity
Structure deposition date
2005-11-25
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
10
% buried
nan
Peptide accession
P61769
Residue number A
45
Residue number B
91
Peptide name
Beta-2-microglobulin
Ligandability
Cysteine 45 of Beta-2-microglobulin
Cysteine 91 of Beta-2-microglobulin
Cysteine 91 in protein B could not be asigned to a Uniprot residue.
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