Ig-like domain-containing protein

Intermolecular

Cysteine 243 of Epididymis luminal protein 214 and cysteine 236

Intramolecular

A redox-regulated disulphide may form between cysteine 243 of Epididymis luminal protein 214 and cysteine 236 of Ig-like domain-containing protein (216 and 214 respectively in this structure).

Details

Redox score ?

PDB code

6mxr

Structure name

crystal structure of the dimeric bh1-fab variant [hc-y33w,hc-d98m,hc- g99m]

Structure deposition date

2018-10-31

Thiol separation (Å)

Half-sphere exposure sum ?

nan

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Epididymis luminal protein 214

Peptide B name

Ig-like domain-containing protein

Peptide A accession

V9HW68

Peptide B accession

Q7Z3Y4

Peptide A residue number

243

Peptide B residue number

236

Ligandability

Cysteine 243 of Epididymis luminal protein 214

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 236 of Ig-like domain-containing protein

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.

A redox-regulated disulphide may form within Ig-like domain-containing protein between cysteines 45 and 110 (23 and 88 respectively in this structure).

Details

Redox score ?

PDB code

5vl7

Structure name

pcsk9 complex with fab33

Structure deposition date

2017-04-25

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Q7Z3Y4

Residue number A

Residue number B

110

Peptide name

Ig-like domain-containing protein

Ligandability

Cysteine 45 of Ig-like domain-containing protein

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 of Ig-like domain-containing protein

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.

A redox-regulated disulphide may form within Ig-like domain-containing protein between cysteines 156 and 216 (134 and 194 respectively in this structure).