Isoform 3 of Endonuclease III-like protein 1
Intramolecular
Cysteine 282 and cysteine 291 L
Cysteine 297 and cysteine 300 L
Cysteine 285 and cysteine 291 L
Cysteine 290 and cysteine 306 L
Cysteine 290 and cysteine 300 L
Cysteine 290 and cysteine 297 L
7rdt A 290 A 299
A redox-regulated disulphide may form within Isoform 3 of Endonuclease III-like protein 1 between cysteines 282 and 291 (290 and 299 respectively in this structure).
Details
Redox score ?
64
PDB code
7rdt
Structure name
structure of human nthl1 - linker 1 chimera
Structure deposition date
2021-07-11
Thiol separation (Å)
6
Half-sphere exposure sum ?
57
Minimum pKa ?
10
% buried
29
Peptide accession
P78549-3
Residue number A
282
Residue number B
291
Peptide name
Isoform 3 of Endonuclease III-like protein 1
Ligandability
Cysteine 282 of Isoform 3 of Endonuclease III-like protein 1
Cysteine 291 of Isoform 3 of Endonuclease III-like protein 1
7rds A 297 A 300
A redox-regulated disulphide may form within Endonuclease III-like protein 1 between cysteines 297 and 300.
Details
Redox score ?
61
PDB code
7rds
Structure name
structure of human nthl1
Structure deposition date
2021-07-11
Thiol separation (Å)
6
Half-sphere exposure sum ?
58
Minimum pKa ?
11
% buried
40
Peptide accession
P78549
Residue number A
297
Residue number B
300
Peptide name
Endonuclease III-like protein 1
Ligandability
Cysteine 297 of Endonuclease III-like protein 1
Cysteine 300 of Endonuclease III-like protein 1
7rdt A 293 A 299
A redox-regulated disulphide may form within Isoform 3 of Endonuclease III-like protein 1 between cysteines 285 and 291 (293 and 299 respectively in this structure).
Details
Redox score ?
60
PDB code
7rdt
Structure name
structure of human nthl1 - linker 1 chimera
Structure deposition date
2021-07-11
Thiol separation (Å)
7
Half-sphere exposure sum ?
56
Minimum pKa ?
10
% buried
48
Peptide accession
P78549-3
Residue number A
285
Residue number B
291
Peptide name
Isoform 3 of Endonuclease III-like protein 1
Ligandability
Cysteine 285 of Isoform 3 of Endonuclease III-like protein 1
Cysteine 291 of Isoform 3 of Endonuclease III-like protein 1
7rds A 290 A 306
A redox-regulated disulphide may form within Endonuclease III-like protein 1 between cysteines 290 and 306. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
58
PDB code
7rds
Structure name
structure of human nthl1
Structure deposition date
2021-07-11
Thiol separation (Å)
6
Half-sphere exposure sum ?
72
Minimum pKa ?
10
% buried
68
Peptide accession
P78549
Residue number A
290
Residue number B
306
Peptide name
Endonuclease III-like protein 1
Ligandability
Cysteine 290 of Endonuclease III-like protein 1
Cysteine 306 of Endonuclease III-like protein 1
7rds A 290 A 300
A redox-regulated disulphide may form within Endonuclease III-like protein 1 between cysteines 290 and 300. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
57
PDB code
7rds
Structure name
structure of human nthl1
Structure deposition date
2021-07-11
Thiol separation (Å)
7
Half-sphere exposure sum ?
67
Minimum pKa ?
10
% buried
67
Peptide accession
P78549
Residue number A
290
Residue number B
300
Peptide name
Endonuclease III-like protein 1
Ligandability
Cysteine 290 of Endonuclease III-like protein 1
Cysteine 300 of Endonuclease III-like protein 1
7rds A 290 A 297
A redox-regulated disulphide may form within Endonuclease III-like protein 1 between cysteines 290 and 297. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
56
PDB code
7rds
Structure name
structure of human nthl1
Structure deposition date
2021-07-11
Thiol separation (Å)
7
Half-sphere exposure sum ?
71
Minimum pKa ?
10
% buried
50
Peptide accession
P78549
Residue number A
290
Residue number B
297
Peptide name
Endonuclease III-like protein 1
Ligandability
Cysteine 290 of Endonuclease III-like protein 1
Cysteine 297 of Endonuclease III-like protein 1
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