Copper-transporting ATPase 1
Intermolecular
Cysteine 12 of Copper transport protein ATOX1 and cysteine 19 L
Cysteine 12 of Copper transport protein ATOX1 and cysteine 22 L
Cysteine 15 of Copper transport protein ATOX1 and cysteine 22 L
Cysteine 15 of Copper transport protein ATOX1 and cysteine 19 L
Intramolecular
Cysteine 182 and cysteine 185
Cysteine 19 and cysteine 22
Cysteine 388 and cysteine 391
Cysteine 288 and cysteine 291
Cysteine 1108 and cysteine 1121
Cysteine 1121 and cysteine 1223
3cjk A 12 B 15
A redox-regulated disulphide may form between cysteine 12 of Copper transport protein ATOX1 and cysteine 19 of Copper-transporting ATPase 1 (12 and 15 respectively in this structure).
Details
Redox score ?
80
PDB code
3cjk
Structure name
crystal structure of the adduct hah1-cd(ii)-mnk1
Structure deposition date
2008-03-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
5
% buried
12
Peptide A name
Copper transport protein ATOX1
Peptide B name
Copper-transporting ATPase 1
Peptide A accession
O00244
Peptide B accession
Q04656
Peptide A residue number
12
Peptide B residue number
19
Ligandability
Cysteine 12 of Copper transport protein ATOX1
Cysteine 19 of Copper-transporting ATPase 1
3cjk A 12 B 18
A redox-regulated disulphide may form between cysteine 12 of Copper transport protein ATOX1 and cysteine 22 of Copper-transporting ATPase 1 (12 and 18 respectively in this structure).
Details
Redox score ?
76
PDB code
3cjk
Structure name
crystal structure of the adduct hah1-cd(ii)-mnk1
Structure deposition date
2008-03-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
8
% buried
33
Peptide A name
Copper transport protein ATOX1
Peptide B name
Copper-transporting ATPase 1
Peptide A accession
O00244
Peptide B accession
Q04656
Peptide A residue number
12
Peptide B residue number
22
Ligandability
Cysteine 12 of Copper transport protein ATOX1
Cysteine 22 of Copper-transporting ATPase 1
5t7l A 15 B 18
A redox-regulated disulphide may form between cysteine 15 of Copper transport protein ATOX1 and cysteine 22 of Copper-transporting ATPase 1 (15 and 18 respectively in this structure).
Details
Redox score ?
68
PDB code
5t7l
Structure name
pt(ii)-mediated copper-dependent interactions between atox1 and mnk1
Structure deposition date
2016-09-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide A name
Copper transport protein ATOX1
Peptide B name
Copper-transporting ATPase 1
Peptide A accession
O00244
Peptide B accession
Q04656
Peptide A residue number
15
Peptide B residue number
22
Ligandability
Cysteine 15 of Copper transport protein ATOX1
Cysteine 22 of Copper-transporting ATPase 1
3cjk A 15 B 15
A redox-regulated disulphide may form between cysteine 15 of Copper transport protein ATOX1 and cysteine 19 of Copper-transporting ATPase 1 (15 and 15 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
3cjk
Structure name
crystal structure of the adduct hah1-cd(ii)-mnk1
Structure deposition date
2008-03-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
61
Minimum pKa ?
5
% buried
32
Peptide A name
Copper transport protein ATOX1
Peptide B name
Copper-transporting ATPase 1
Peptide A accession
O00244
Peptide B accession
Q04656
Peptide A residue number
15
Peptide B residue number
19
Ligandability
Cysteine 15 of Copper transport protein ATOX1
Cysteine 19 of Copper-transporting ATPase 1
1s6u A 14 A 17
A redox-regulated disulphide may form within Copper-transporting ATPase 1 between cysteines 182 and 185 (14 and 17 respectively in this structure).
Details
Redox score ?
80
PDB code
1s6u
Structure name
solution structure and backbone dynamics of the cu(i) form of the second metal-binding domain of the menkes protein atp7a
Structure deposition date
2004-01-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
44
Minimum pKa ?
8
% buried
0
Peptide accession
Q04656
Residue number A
182
Residue number B
185
Peptide name
Copper-transporting ATPase 1
Ligandability
Cysteine 182 of Copper-transporting ATPase 1
Cysteine 185 of Copper-transporting ATPase 1
3cjk B 15 B 18
A redox-regulated disulphide may form within Copper-transporting ATPase 1 between cysteines 19 and 22 (15 and 18 respectively in this structure).
Details
Redox score ?
78
PDB code
3cjk
Structure name
crystal structure of the adduct hah1-cd(ii)-mnk1
Structure deposition date
2008-03-13
Thiol separation (Å)
5
Half-sphere exposure sum ?
57
Minimum pKa ?
5
% buried
22
Peptide accession
Q04656
Residue number A
19
Residue number B
22
Peptide name
Copper-transporting ATPase 1
Ligandability
Cysteine 19 of Copper-transporting ATPase 1
Cysteine 22 of Copper-transporting ATPase 1
2aw0 A 14 A 17
A redox-regulated disulphide may form within Copper-transporting ATPase 1 between cysteines 388 and 391 (14 and 17 respectively in this structure).
Details
Redox score ?
66
PDB code
2aw0
Structure name
fourth metal-binding domain of the menkes copper-transporting atpase, nmr, 20 structures
Structure deposition date
1997-10-08
Thiol separation (Å)
5
Half-sphere exposure sum ?
44
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q04656
Residue number A
388
Residue number B
391
Peptide name
Copper-transporting ATPase 1
Ligandability
Cysteine 388 of Copper-transporting ATPase 1
Cysteine 391 of Copper-transporting ATPase 1
2g9o A 14 A 17
A redox-regulated disulphide may form within Copper-transporting ATPase 1 between cysteines 288 and 291 (14 and 17 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
2g9o
Structure name
solution structure of the apo form of the third metal-binding domain of atp7a protein (menkes disease protein)
Structure deposition date
2006-03-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
51
Minimum pKa ?
9
% buried
4
Peptide accession
Q04656
Residue number A
288
Residue number B
291
Peptide name
Copper-transporting ATPase 1
Ligandability
Cysteine 288 of Copper-transporting ATPase 1
Cysteine 291 of Copper-transporting ATPase 1
2kmx A 1108 A 1121
A redox-regulated disulphide may form within Copper-transporting ATPase 1 between cysteines 1108 and 1121. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
35
PDB code
2kmx
Structure name
solution structure of the nucleotide binding domain of the human menkes protein in the atp-bound form
Structure deposition date
2009-08-05
Thiol separation (Å)
10
Half-sphere exposure sum ?
63
Minimum pKa ?
10
% buried
60
Peptide accession
Q04656
Residue number A
1108
Residue number B
1121
Peptide name
Copper-transporting ATPase 1
Ligandability
Cysteine 1108 of Copper-transporting ATPase 1
Cysteine 1121 of Copper-transporting ATPase 1
2kmv A 1121 A 1223
A redox-regulated disulphide may form within Copper-transporting ATPase 1 between cysteines 1121 and 1223. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
2kmv
Structure name
solution structure of the nucleotide binding domain of the human menkes protein in the atp-free form
Structure deposition date
2009-08-05
Thiol separation (Å)
10
Half-sphere exposure sum ?
68
Minimum pKa ?
11
% buried
68
Peptide accession
Q04656
Residue number A
1121
Residue number B
1223
Peptide name
Copper-transporting ATPase 1
Ligandability
Cysteine 1121 of Copper-transporting ATPase 1
Cysteine 1223 of Copper-transporting ATPase 1
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