ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

Macrophage migration inhibitory factor

Intermolecular
Cysteine 81 and cysteine 110 L
Intramolecular
Cysteine 60 and cysteine 81 L
Cysteine 57 and cysteine 60
A redox-regulated disulphide may form between two units of Macrophage migration inhibitory factor at cysteines 81 and 110 (80 and 110 respectively in this structure).

Details

Redox score ?
85
PDB code
4gum
Structure name
cystal structure of locked-trimer of human mif
Structure deposition date
2012-08-29
Thiol separation (Å)
2
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide A name
Macrophage migration inhibitory factor
Peptide B name
Macrophage migration inhibitory factor
Peptide A accession
P14174
Peptide B accession
P14174
Peptide A residue number
81
Peptide B residue number
110

Ligandability

Cysteine 81 of Macrophage migration inhibitory factor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

Cysteine 110 of Macrophage migration inhibitory factor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 110 in protein B could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within Macrophage migration inhibitory factor between cysteines 60 and 81 (59 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 ?
42
PDB code
4gum
Structure name
cystal structure of locked-trimer of human mif
Structure deposition date
2012-08-29
Thiol separation (Å)
8
Half-sphere exposure sum ?
74
Minimum pKa ?
13
% buried
nan
Peptide accession
P14174
Residue number A
60
Residue number B
81
Peptide name
Macrophage migration inhibitory factor

Ligandability

Cysteine 60 of Macrophage migration inhibitory factor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 81 of Macrophage migration inhibitory factor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Macrophage migration inhibitory factor between cysteines 57 and 60 (56 and 59 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
30
PDB code
3l5s
Structure name
crystal structure of macrophage migration inhibitory factor (mif) with imidazopyrimidinylphenyl inhibitor at 1
Structure deposition date
2009-12-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
79
Minimum pKa ?
12
% buried
90
Peptide accession
P14174
Residue number A
57
Residue number B
60
Peptide name
Macrophage migration inhibitory factor

Ligandability

Cysteine 57 of Macrophage migration inhibitory factor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 60 of Macrophage migration inhibitory factor

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

If this tool was useful for finding a disulphide, please cite: