NAD(+) hydrolase SARM1
Intermolecular
Cysteine 649 and cysteine 649
Intramolecular
Cysteine 508 and cysteine 527
Cysteine 215 and cysteine 226
Cysteine 199 and cysteine 233
Cysteine 629 and cysteine 635
Cysteine 215 and cysteine 233
Cysteine 271 and cysteine 343
6o0v A 649 C 649
A redox-regulated disulphide may form between two units of NAD(+) hydrolase SARM1 at cysteines 649 and 649. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
59
PDB code
6o0v
Structure name
crystal structure of the tir domain g601p mutant from human sarm1, crystal form 2
Structure deposition date
2019-02-17
Thiol separation (Å)
5
Half-sphere exposure sum ?
73
Minimum pKa ?
11
% buried
77
Peptide A name
NAD(+) hydrolase SARM1
Peptide B name
NAD(+) hydrolase SARM1
Peptide A accession
Q6SZW1
Peptide B accession
Q6SZW1
Peptide A residue number
649
Peptide B residue number
649
Ligandability
6qwv L 508 L 527
A redox-regulated disulphide may form within NAD(+) hydrolase SARM1 between cysteines 508 and 527.
Details
Redox score ?
74
PDB code
6qwv
Structure name
sarm1 sam1-2 domains
Structure deposition date
2019-03-06
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
9
% buried
90
Peptide accession
Q6SZW1
Residue number A
508
Residue number B
527
Peptide name
NAD(+) hydrolase SARM1
Ligandability
Cysteine 508 of NAD(+) hydrolase SARM1
Cysteine 527 of NAD(+) hydrolase SARM1
7nal F 215 F 226
A redox-regulated disulphide may form within NAD(+) hydrolase SARM1 between cysteines 215 and 226.
Details
Redox score ?
69
PDB code
7nal
Structure name
cryo-em structure of activated human sarm1 in complex with nmn and 1ad (arm and sam domains)
Structure deposition date
2021-06-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
83
Minimum pKa ?
8
% buried
94
Peptide accession
Q6SZW1
Residue number A
215
Residue number B
226
Peptide name
NAD(+) hydrolase SARM1
Ligandability
Cysteine 215 of NAD(+) hydrolase SARM1
Cysteine 226 of NAD(+) hydrolase SARM1
7nal C 199 C 233
A redox-regulated disulphide may form within NAD(+) hydrolase SARM1 between cysteines 199 and 233. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
7nal
Structure name
cryo-em structure of activated human sarm1 in complex with nmn and 1ad (arm and sam domains)
Structure deposition date
2021-06-21
Thiol separation (Å)
7
Half-sphere exposure sum ?
81
Minimum pKa ?
11
% buried
86
Peptide accession
Q6SZW1
Residue number A
199
Residue number B
233
Peptide name
NAD(+) hydrolase SARM1
Ligandability
Cysteine 199 of NAD(+) hydrolase SARM1
Cysteine 233 of NAD(+) hydrolase SARM1
8d0i B 629 B 635
A redox-regulated disulphide may form within NAD(+) hydrolase SARM1 between cysteines 629 and 635. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
8d0i
Structure name
human sarm1 bound to an nb-3 eadpr adduct
Structure deposition date
2022-05-26
Thiol separation (Å)
9
Half-sphere exposure sum ?
52
Minimum pKa ?
10
% buried
52
Peptide accession
Q6SZW1
Residue number A
629
Residue number B
635
Peptide name
NAD(+) hydrolase SARM1
Ligandability
Cysteine 629 of NAD(+) hydrolase SARM1
Cysteine 635 of NAD(+) hydrolase SARM1
7nal D 215 D 233
A redox-regulated disulphide may form within NAD(+) hydrolase SARM1 between cysteines 215 and 233. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
7nal
Structure name
cryo-em structure of activated human sarm1 in complex with nmn and 1ad (arm and sam domains)
Structure deposition date
2021-06-21
Thiol separation (Å)
10
Half-sphere exposure sum ?
81
Minimum pKa ?
8
% buried
95
Peptide accession
Q6SZW1
Residue number A
215
Residue number B
233
Peptide name
NAD(+) hydrolase SARM1
Ligandability
Cysteine 215 of NAD(+) hydrolase SARM1
Cysteine 233 of NAD(+) hydrolase SARM1
8gnj A 271 A 343
A redox-regulated disulphide may form within NAD(+) hydrolase SARM1 between cysteines 271 and 343. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
8gnj
Structure name
human sarm1 bounded with nmn and nanobody-c6, conformation 2
Structure deposition date
2022-08-24
Thiol separation (Å)
8
Half-sphere exposure sum ?
83
Minimum pKa ?
11
% buried
74
Peptide accession
Q6SZW1
Residue number A
271
Residue number B
343
Peptide name
NAD(+) hydrolase SARM1
Ligandability
Cysteine 271 of NAD(+) hydrolase SARM1
Cysteine 343 of NAD(+) hydrolase SARM1
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