N-formyl peptide receptor 2
Intermolecular
Cysteine 126 and cysteine 351 of Guanine nucleotide-binding protein G(i) subunit alpha-1
Cysteine 126 and cysteine 352 of Guanine nucleotide-binding protein G(i) subunit alpha-2
Cysteine 63 and cysteine 352 of Guanine nucleotide-binding protein G(i) subunit alpha-2
Cysteine 351 of Guanine nucleotide-binding protein G(i) subunit alpha-1 and cysteine 63
Intramolecular
Cysteine 124 and cysteine 220
Cysteine 98 and cysteine 176
Cysteine 124 and cysteine 126
Cysteine 253 and cysteine 296
Cysteine 63 and cysteine 126
6omm R 126 A 351
A redox-regulated disulphide may form between cysteine 126 of N-formyl peptide receptor 2 and cysteine 351 of Guanine nucleotide-binding protein G(i) subunit alpha-1. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
56
PDB code
6omm
Structure name
cryo-em structure of formyl peptide receptor 2/lipoxin a4 receptor in complex with gi
Structure deposition date
2019-04-19
Thiol separation (Å)
5
Half-sphere exposure sum ?
75
Minimum pKa ?
11
% buried
100
Peptide A name
N-formyl peptide receptor 2
Peptide B name
Guanine nucleotide-binding protein G(i) subunit alpha-1
Peptide A accession
P25090
Peptide B accession
P63096
Peptide A residue number
126
Peptide B residue number
351
Ligandability
Cysteine 126 of N-formyl peptide receptor 2
Cysteine 351 of Guanine nucleotide-binding protein G(i) subunit alpha-1
7wvv R 126 A 352
A redox-regulated disulphide may form between cysteine 126 of N-formyl peptide receptor 2 and cysteine 352 of Guanine nucleotide-binding protein G(i) subunit alpha-2. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
7wvv
Structure name
cryo-em structure of the human formyl peptide receptor 2 in complex with fmlfii and gi2
Structure deposition date
2022-02-11
Thiol separation (Å)
8
Half-sphere exposure sum ?
74
Minimum pKa ?
10
% buried
93
Peptide A name
N-formyl peptide receptor 2
Peptide B name
Guanine nucleotide-binding protein G(i) subunit alpha-2
Peptide A accession
P25090
Peptide B accession
P04899
Peptide A residue number
126
Peptide B residue number
352
Ligandability
Cysteine 126 of N-formyl peptide receptor 2
Cysteine 352 of Guanine nucleotide-binding protein G(i) subunit alpha-2
7wvy R 63 A 352
A redox-regulated disulphide may form between cysteine 63 of N-formyl peptide receptor 2 and cysteine 352 of Guanine nucleotide-binding protein G(i) subunit alpha-2. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
35
PDB code
7wvy
Structure name
cryo-em structure of the human formyl peptide receptor 2 in complex with abeta42 and gi2
Structure deposition date
2022-02-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
79
Minimum pKa ?
10
% buried
94
Peptide A name
N-formyl peptide receptor 2
Peptide B name
Guanine nucleotide-binding protein G(i) subunit alpha-2
Peptide A accession
P25090
Peptide B accession
P04899
Peptide A residue number
63
Peptide B residue number
352
Ligandability
Cysteine 63 of N-formyl peptide receptor 2
Cysteine 352 of Guanine nucleotide-binding protein G(i) subunit alpha-2
7t6s A 351 R 63
A redox-regulated disulphide may form between cysteine 351 of Guanine nucleotide-binding protein G(i) subunit alpha-1 and cysteine 63 of N-formyl peptide receptor 2. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
33
PDB code
7t6s
Structure name
molecular recognition of formylpeptides and diverse agonists by the formylpeptide receptors fpr1 and fpr2
Structure deposition date
2021-12-14
Thiol separation (Å)
9
Half-sphere exposure sum ?
80
Minimum pKa ?
11
% buried
96
Peptide A name
Guanine nucleotide-binding protein G(i) subunit alpha-1
Peptide B name
N-formyl peptide receptor 2
Peptide A accession
P63096
Peptide B accession
P25090
Peptide A residue number
351
Peptide B residue number
63
Ligandability
Cysteine 351 of Guanine nucleotide-binding protein G(i) subunit alpha-1
Cysteine 63 of N-formyl peptide receptor 2
6lw5 A 124 A 220
A redox-regulated disulphide may form within N-formyl peptide receptor 2 between cysteines 124 and 220.
Details
Redox score ?
73
PDB code
6lw5
Structure name
crystal structure of the human formyl peptide receptor 2 in complex with wkymvm
Structure deposition date
2020-02-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
10
% buried
32
Peptide accession
P25090
Residue number A
124
Residue number B
220
Peptide name
N-formyl peptide receptor 2
Ligandability
Cysteine 124 of N-formyl peptide receptor 2
Cysteine 220 of N-formyl peptide receptor 2
7t6s R 98 R 176
A redox-regulated disulphide may form within N-formyl peptide receptor 2 between cysteines 98 and 176.
Details
Redox score ?
69
PDB code
7t6s
Structure name
molecular recognition of formylpeptides and diverse agonists by the formylpeptide receptors fpr1 and fpr2
Structure deposition date
2021-12-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
67
Minimum pKa ?
10
% buried
56
Peptide accession
P25090
Residue number A
98
Residue number B
176
Peptide name
N-formyl peptide receptor 2
Ligandability
Cysteine 98 of N-formyl peptide receptor 2
Cysteine 176 of N-formyl peptide receptor 2
6lw5 A 124 A 126
A redox-regulated disulphide may form within N-formyl peptide receptor 2 between cysteines 124 and 126. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
6lw5
Structure name
crystal structure of the human formyl peptide receptor 2 in complex with wkymvm
Structure deposition date
2020-02-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
55
Minimum pKa ?
10
% buried
32
Peptide accession
P25090
Residue number A
124
Residue number B
126
Peptide name
N-formyl peptide receptor 2
Ligandability
Cysteine 124 of N-formyl peptide receptor 2
Cysteine 126 of N-formyl peptide receptor 2
6lw5 A 253 A 296
A redox-regulated disulphide may form within N-formyl peptide receptor 2 between cysteines 253 and 296. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
6lw5
Structure name
crystal structure of the human formyl peptide receptor 2 in complex with wkymvm
Structure deposition date
2020-02-07
Thiol separation (Å)
8
Half-sphere exposure sum ?
74
Minimum pKa ?
11
% buried
68
Peptide accession
P25090
Residue number A
253
Residue number B
296
Peptide name
N-formyl peptide receptor 2
Ligandability
Cysteine 253 of N-formyl peptide receptor 2
Cysteine 296 of N-formyl peptide receptor 2
6lw5 A 63 A 126
A redox-regulated disulphide may form within N-formyl peptide receptor 2 between cysteines 63 and 126. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
6lw5
Structure name
crystal structure of the human formyl peptide receptor 2 in complex with wkymvm
Structure deposition date
2020-02-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
68
Minimum pKa ?
10
% buried
61
Peptide accession
P25090
Residue number A
63
Residue number B
126
Peptide name
N-formyl peptide receptor 2
Ligandability
Cysteine 63 of N-formyl peptide receptor 2
Cysteine 126 of N-formyl peptide receptor 2
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