Copper in PDB 4enz: Structure of Human Ceruloplasmin at 2.6 A Resolution
Enzymatic activity of Structure of Human Ceruloplasmin at 2.6 A Resolution
All present enzymatic activity of Structure of Human Ceruloplasmin at 2.6 A Resolution:
1.16.3.1;
Protein crystallography data
The structure of Structure of Human Ceruloplasmin at 2.6 A Resolution, PDB code: 4enz
was solved by
V.R.Samygina,
A.V.Sokolov,
G.Bourenkov,
V.B.Vasilyev,
H.Bartunik,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
14.90 /
2.60
|
Space group
|
P 32 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
210.775,
210.775,
84.502,
90.00,
90.00,
120.00
|
R / Rfree (%)
|
19.9 /
23.4
|
Other elements in 4enz:
The structure of Structure of Human Ceruloplasmin at 2.6 A Resolution also contains other interesting chemical elements:
Copper Binding Sites:
The binding sites of Copper atom in the Structure of Human Ceruloplasmin at 2.6 A Resolution
(pdb code 4enz). This binding sites where shown within
5.0 Angstroms radius around Copper atom.
In total 6 binding sites of Copper where determined in the
Structure of Human Ceruloplasmin at 2.6 A Resolution, PDB code: 4enz:
Jump to Copper binding site number:
1;
2;
3;
4;
5;
6;
Copper binding site 1 out
of 6 in 4enz
Go back to
Copper Binding Sites List in 4enz
Copper binding site 1 out
of 6 in the Structure of Human Ceruloplasmin at 2.6 A Resolution
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 1 of Structure of Human Ceruloplasmin at 2.6 A Resolution within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu1102
b:66.4
occ:1.00
|
ND1
|
A:HIS324
|
1.9
|
62.1
|
1.0
|
ND1
|
A:HIS276
|
1.9
|
66.1
|
1.0
|
SG
|
A:CYS319
|
2.1
|
67.6
|
1.0
|
CE1
|
A:HIS324
|
2.9
|
62.8
|
1.0
|
CE1
|
A:HIS276
|
2.9
|
65.5
|
1.0
|
CG
|
A:HIS276
|
3.0
|
65.0
|
1.0
|
CG
|
A:HIS324
|
3.0
|
66.0
|
1.0
|
CB
|
A:CYS319
|
3.2
|
67.9
|
1.0
|
CD1
|
A:LEU329
|
3.2
|
66.1
|
1.0
|
CB
|
A:HIS276
|
3.3
|
64.4
|
1.0
|
CA
|
A:HIS276
|
3.4
|
63.5
|
1.0
|
CB
|
A:HIS324
|
3.4
|
67.3
|
1.0
|
O
|
A:VAL275
|
3.9
|
64.0
|
1.0
|
NE2
|
A:HIS324
|
4.0
|
62.6
|
1.0
|
NE2
|
A:HIS276
|
4.0
|
64.2
|
1.0
|
CD2
|
A:HIS276
|
4.1
|
64.2
|
1.0
|
CD2
|
A:HIS324
|
4.1
|
65.9
|
1.0
|
CB
|
A:ASN321
|
4.1
|
65.6
|
1.0
|
N
|
A:HIS276
|
4.2
|
62.0
|
1.0
|
N
|
A:ALA277
|
4.3
|
63.0
|
1.0
|
C
|
A:VAL275
|
4.4
|
62.7
|
1.0
|
C
|
A:HIS276
|
4.4
|
62.5
|
1.0
|
CG
|
A:LEU329
|
4.5
|
66.9
|
1.0
|
CA
|
A:CYS319
|
4.5
|
68.5
|
1.0
|
ND2
|
A:ASN321
|
4.8
|
64.3
|
1.0
|
CD2
|
A:PHE202
|
4.8
|
62.9
|
1.0
|
CB
|
A:LEU329
|
4.8
|
69.0
|
1.0
|
CG
|
A:ASN321
|
4.8
|
65.3
|
1.0
|
CA
|
A:HIS324
|
4.9
|
68.3
|
1.0
|
|
Copper binding site 2 out
of 6 in 4enz
Go back to
Copper Binding Sites List in 4enz
Copper binding site 2 out
of 6 in the Structure of Human Ceruloplasmin at 2.6 A Resolution
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 2 of Structure of Human Ceruloplasmin at 2.6 A Resolution within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu1103
b:59.3
occ:1.00
|
NE2
|
A:HIS1020
|
2.0
|
47.7
|
1.0
|
NE2
|
A:HIS980
|
2.1
|
47.8
|
1.0
|
NE2
|
A:HIS163
|
2.1
|
58.1
|
1.0
|
O2
|
A:OXY1109
|
2.6
|
66.1
|
1.0
|
O1
|
A:OXY1109
|
2.7
|
66.2
|
1.0
|
CD2
|
A:HIS1020
|
2.9
|
49.4
|
1.0
|
CE1
|
A:HIS980
|
2.9
|
47.7
|
1.0
|
CD2
|
A:HIS163
|
2.9
|
59.6
|
1.0
|
CE1
|
A:HIS1020
|
3.0
|
49.1
|
1.0
|
CD2
|
A:HIS980
|
3.1
|
47.8
|
1.0
|
CE1
|
A:HIS163
|
3.2
|
58.9
|
1.0
|
CD2
|
A:LEU1018
|
4.0
|
52.5
|
1.0
|
CG
|
A:HIS1020
|
4.1
|
52.2
|
1.0
|
ND1
|
A:HIS1020
|
4.1
|
47.9
|
1.0
|
ND1
|
A:HIS980
|
4.1
|
45.8
|
1.0
|
CG
|
A:HIS163
|
4.2
|
58.9
|
1.0
|
CG
|
A:HIS980
|
4.2
|
48.9
|
1.0
|
ND1
|
A:HIS163
|
4.2
|
56.9
|
1.0
|
CD2
|
A:HIS978
|
4.3
|
53.7
|
1.0
|
CU
|
A:CU1104
|
4.5
|
60.7
|
1.0
|
NE2
|
A:HIS101
|
4.7
|
55.0
|
1.0
|
NE2
|
A:HIS978
|
4.9
|
55.8
|
1.0
|
CG
|
A:LEU1018
|
4.9
|
53.7
|
1.0
|
|
Copper binding site 3 out
of 6 in 4enz
Go back to
Copper Binding Sites List in 4enz
Copper binding site 3 out
of 6 in the Structure of Human Ceruloplasmin at 2.6 A Resolution
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 3 of Structure of Human Ceruloplasmin at 2.6 A Resolution within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu1104
b:60.7
occ:1.00
|
NE2
|
A:HIS101
|
2.1
|
55.0
|
1.0
|
NE2
|
A:HIS978
|
2.2
|
55.8
|
1.0
|
O2
|
A:OXY1109
|
2.3
|
66.1
|
1.0
|
CE1
|
A:HIS101
|
3.0
|
55.2
|
1.0
|
CD2
|
A:HIS978
|
3.1
|
53.7
|
1.0
|
CD2
|
A:HIS101
|
3.1
|
55.8
|
1.0
|
CE1
|
A:HIS978
|
3.1
|
56.1
|
1.0
|
O
|
A:O1108
|
3.2
|
22.1
|
0.5
|
O1
|
A:OXY1109
|
3.3
|
66.2
|
1.0
|
NE2
|
A:HIS103
|
3.4
|
57.1
|
1.0
|
CD2
|
A:HIS103
|
3.5
|
60.9
|
1.0
|
NE2
|
A:HIS980
|
3.5
|
47.8
|
1.0
|
CD2
|
A:HIS980
|
3.6
|
47.8
|
1.0
|
CE1
|
A:HIS980
|
3.7
|
47.7
|
1.0
|
CE1
|
A:HIS103
|
3.8
|
56.7
|
1.0
|
CG
|
A:HIS980
|
3.8
|
48.9
|
1.0
|
CG
|
A:HIS103
|
3.9
|
60.0
|
1.0
|
ND1
|
A:HIS980
|
3.9
|
45.8
|
1.0
|
ND1
|
A:HIS103
|
4.0
|
55.5
|
1.0
|
ND1
|
A:HIS101
|
4.1
|
56.7
|
1.0
|
CG
|
A:HIS101
|
4.2
|
57.9
|
1.0
|
ND1
|
A:HIS978
|
4.2
|
53.9
|
1.0
|
CG
|
A:HIS978
|
4.3
|
53.0
|
1.0
|
CA
|
A:HIS980
|
4.4
|
50.9
|
1.0
|
CU
|
A:CU1105
|
4.4
|
62.6
|
1.0
|
CU
|
A:CU1103
|
4.5
|
59.3
|
1.0
|
OH
|
A:TYR107
|
4.5
|
62.3
|
1.0
|
CA
|
A:HIS103
|
4.5
|
63.4
|
1.0
|
CB
|
A:HIS980
|
4.6
|
51.0
|
1.0
|
O
|
A:SER102
|
4.7
|
64.6
|
1.0
|
CB
|
A:HIS103
|
4.8
|
62.6
|
1.0
|
O
|
A:PHE979
|
4.9
|
53.3
|
1.0
|
N
|
A:HIS980
|
5.0
|
50.9
|
1.0
|
|
Copper binding site 4 out
of 6 in 4enz
Go back to
Copper Binding Sites List in 4enz
Copper binding site 4 out
of 6 in the Structure of Human Ceruloplasmin at 2.6 A Resolution
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 4 of Structure of Human Ceruloplasmin at 2.6 A Resolution within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu1105
b:62.6
occ:1.00
|
NE2
|
A:HIS103
|
1.7
|
57.1
|
1.0
|
NE2
|
A:HIS1022
|
1.8
|
53.2
|
1.0
|
NE2
|
A:HIS161
|
1.9
|
54.5
|
1.0
|
O1
|
A:OXY1109
|
2.4
|
66.2
|
1.0
|
CE1
|
A:HIS103
|
2.4
|
56.7
|
1.0
|
CE1
|
A:HIS1022
|
2.7
|
57.4
|
1.0
|
CE1
|
A:HIS161
|
2.8
|
55.8
|
1.0
|
CD2
|
A:HIS1022
|
2.8
|
53.9
|
1.0
|
CD2
|
A:HIS103
|
3.0
|
60.9
|
1.0
|
CD2
|
A:HIS161
|
3.0
|
57.5
|
1.0
|
O2
|
A:OXY1109
|
3.2
|
66.1
|
1.0
|
ND1
|
A:HIS103
|
3.6
|
55.5
|
1.0
|
ND1
|
A:HIS1022
|
3.9
|
55.0
|
1.0
|
CG
|
A:HIS103
|
3.9
|
60.0
|
1.0
|
ND1
|
A:HIS161
|
3.9
|
55.9
|
1.0
|
CG
|
A:HIS1022
|
3.9
|
53.6
|
1.0
|
CG
|
A:HIS161
|
4.1
|
57.2
|
1.0
|
CD1
|
A:ILE159
|
4.1
|
49.4
|
1.0
|
CD2
|
A:HIS978
|
4.4
|
53.7
|
1.0
|
CU
|
A:CU1104
|
4.4
|
60.7
|
1.0
|
NE2
|
A:HIS978
|
4.5
|
55.8
|
1.0
|
CD2
|
A:HIS101
|
4.7
|
55.8
|
1.0
|
CG1
|
A:ILE159
|
4.7
|
55.9
|
1.0
|
|
Copper binding site 5 out
of 6 in 4enz
Go back to
Copper Binding Sites List in 4enz
Copper binding site 5 out
of 6 in the Structure of Human Ceruloplasmin at 2.6 A Resolution
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 5 of Structure of Human Ceruloplasmin at 2.6 A Resolution within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu1106
b:61.5
occ:1.00
|
ND1
|
A:HIS685
|
1.9
|
52.5
|
1.0
|
ND1
|
A:HIS637
|
2.0
|
59.6
|
1.0
|
SG
|
A:CYS680
|
2.2
|
52.8
|
1.0
|
SD
|
A:MET690
|
2.8
|
58.9
|
1.0
|
CE1
|
A:HIS685
|
2.8
|
55.3
|
1.0
|
CE1
|
A:HIS637
|
2.9
|
61.0
|
1.0
|
CG
|
A:HIS685
|
2.9
|
54.0
|
1.0
|
CG
|
A:HIS637
|
3.0
|
56.5
|
1.0
|
CB
|
A:CYS680
|
3.2
|
53.5
|
1.0
|
OG1
|
A:THR682
|
3.3
|
61.4
|
1.0
|
CB
|
A:HIS685
|
3.4
|
55.2
|
1.0
|
CB
|
A:HIS637
|
3.4
|
56.7
|
1.0
|
CA
|
A:HIS637
|
3.5
|
55.9
|
1.0
|
CE
|
A:MET690
|
3.7
|
58.3
|
1.0
|
NE2
|
A:HIS685
|
4.0
|
54.8
|
1.0
|
CD2
|
A:HIS685
|
4.0
|
53.7
|
1.0
|
O
|
A:VAL636
|
4.0
|
55.9
|
1.0
|
NE2
|
A:HIS637
|
4.0
|
58.9
|
1.0
|
CD2
|
A:HIS637
|
4.1
|
57.2
|
1.0
|
CG
|
A:MET690
|
4.4
|
55.7
|
1.0
|
CG2
|
A:THR682
|
4.4
|
51.4
|
1.0
|
N
|
A:HIS637
|
4.4
|
56.5
|
1.0
|
CB
|
A:THR682
|
4.5
|
54.3
|
1.0
|
N
|
A:GLY638
|
4.5
|
53.4
|
1.0
|
C
|
A:HIS637
|
4.5
|
54.9
|
1.0
|
C
|
A:VAL636
|
4.5
|
57.0
|
1.0
|
CA
|
A:CYS680
|
4.5
|
52.6
|
1.0
|
CD1
|
A:ILE639
|
4.7
|
51.1
|
1.0
|
CA
|
A:HIS685
|
4.9
|
55.5
|
1.0
|
|
Copper binding site 6 out
of 6 in 4enz
Go back to
Copper Binding Sites List in 4enz
Copper binding site 6 out
of 6 in the Structure of Human Ceruloplasmin at 2.6 A Resolution
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 6 of Structure of Human Ceruloplasmin at 2.6 A Resolution within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu1107
b:62.7
occ:1.00
|
ND1
|
A:HIS1026
|
2.0
|
53.9
|
1.0
|
ND1
|
A:HIS975
|
2.1
|
50.9
|
1.0
|
SG
|
A:CYS1021
|
2.3
|
56.1
|
1.0
|
CE1
|
A:HIS1026
|
2.9
|
54.8
|
1.0
|
CG
|
A:HIS1026
|
3.0
|
54.5
|
1.0
|
CE1
|
A:HIS975
|
3.0
|
50.4
|
1.0
|
O
|
A:LEU974
|
3.1
|
54.7
|
1.0
|
CG
|
A:HIS975
|
3.1
|
50.2
|
1.0
|
CB
|
A:CYS1021
|
3.2
|
54.3
|
1.0
|
CB
|
A:HIS1026
|
3.3
|
55.1
|
1.0
|
SD
|
A:MET1031
|
3.3
|
62.0
|
1.0
|
CA
|
A:HIS975
|
3.4
|
51.1
|
1.0
|
CB
|
A:HIS975
|
3.5
|
50.5
|
1.0
|
CG1
|
A:VAL1023
|
3.7
|
53.6
|
1.0
|
C
|
A:LEU974
|
3.9
|
53.5
|
1.0
|
NE2
|
A:HIS1026
|
4.1
|
53.6
|
1.0
|
CD2
|
A:HIS1026
|
4.1
|
53.1
|
1.0
|
N
|
A:HIS975
|
4.1
|
51.6
|
1.0
|
NE2
|
A:HIS975
|
4.2
|
50.4
|
1.0
|
CD2
|
A:HIS975
|
4.2
|
48.4
|
1.0
|
CG2
|
A:VAL1023
|
4.4
|
52.8
|
1.0
|
C
|
A:HIS975
|
4.5
|
51.2
|
1.0
|
CB
|
A:VAL1023
|
4.6
|
54.4
|
1.0
|
CE
|
A:MET1031
|
4.6
|
57.1
|
1.0
|
N
|
A:THR976
|
4.6
|
50.5
|
1.0
|
CA
|
A:CYS1021
|
4.6
|
54.2
|
1.0
|
CG
|
A:MET1031
|
4.7
|
56.8
|
1.0
|
CA
|
A:HIS1026
|
4.9
|
56.5
|
1.0
|
|
Reference:
V.R.Samygina,
A.V.Sokolov,
G.Bourenkov,
M.V.Petoukhov,
M.O.Pulina,
E.T.Zakharova,
V.B.Vasilyev,
H.Bartunik,
D.I.Svergun.
Ceruloplasmin: Macromolecular Assemblies with Iron-Containing Acute Phase Proteins. Plos One V. 8 67145 2013.
ISSN: ESSN 1932-6203
PubMed: 23843990
DOI: 10.1371/JOURNAL.PONE.0067145
Page generated: Wed Jul 31 02:50:13 2024
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