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Copper in PDB 1s1q: TSG101(Uev) Domain in Complex with Ubiquitin

Protein crystallography data

The structure of TSG101(Uev) Domain in Complex with Ubiquitin, PDB code: 1s1q was solved by W.I.Sundquist, H.L.Schubert, B.N.Kelly, G.C.Hill, J.M.Holton, C.P.Hill, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 72.55 / 2.00
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 143.634, 59.154, 93.998, 90.00, 128.67, 90.00
R / Rfree (%) 20.1 / 24

Copper Binding Sites:

The binding sites of Copper atom in the TSG101(Uev) Domain in Complex with Ubiquitin (pdb code 1s1q). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 4 binding sites of Copper where determined in the TSG101(Uev) Domain in Complex with Ubiquitin, PDB code: 1s1q:
Jump to Copper binding site number: 1; 2; 3; 4;

Copper binding site 1 out of 4 in 1s1q

Go back to Copper Binding Sites List in 1s1q
Copper binding site 1 out of 4 in the TSG101(Uev) Domain in Complex with Ubiquitin


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of TSG101(Uev) Domain in Complex with Ubiquitin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu9002

b:27.8
occ:1.00
OE2 A:GLU138 1.9 30.4 1.0
NE2 A:HIS102 2.0 24.0 1.0
O A:HOH9023 2.1 25.0 1.0
CD A:GLU138 2.8 31.4 1.0
CE1 A:HIS102 3.0 24.8 1.0
OE1 A:GLU138 3.0 33.0 1.0
CD2 A:HIS102 3.1 19.9 1.0
CD A:LYS101 3.8 27.5 1.0
ND1 A:HIS102 4.1 22.5 1.0
CG A:HIS102 4.2 21.4 1.0
CG A:GLU138 4.2 29.3 1.0
CB A:LYS101 4.4 23.7 1.0
NZ A:LYS101 4.6 32.2 1.0
CE A:LYS101 4.6 30.0 1.0
CG1 A:VAL134 4.6 21.3 1.0
CG A:LYS101 4.8 24.6 1.0

Copper binding site 2 out of 4 in 1s1q

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Copper binding site 2 out of 4 in the TSG101(Uev) Domain in Complex with Ubiquitin


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of TSG101(Uev) Domain in Complex with Ubiquitin within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu9003

b:43.5
occ:1.00
OD1 B:ASP32 2.0 26.6 1.0
CG B:ASP32 3.0 28.4 1.0
OD2 B:ASP32 3.3 30.3 1.0
OE1 B:GLN31 4.1 30.4 1.0
O B:ALA28 4.3 26.4 1.0
CB B:ASP32 4.3 27.4 1.0
CD B:GLN31 4.5 27.9 1.0
CG B:GLN31 4.5 26.9 1.0
CA B:ASP32 4.6 26.9 1.0
N B:ASP32 4.6 26.6 1.0

Copper binding site 3 out of 4 in 1s1q

Go back to Copper Binding Sites List in 1s1q
Copper binding site 3 out of 4 in the TSG101(Uev) Domain in Complex with Ubiquitin


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of TSG101(Uev) Domain in Complex with Ubiquitin within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cu9001

b:27.9
occ:1.00
OE2 C:GLU138 2.0 26.6 1.0
NE2 C:HIS102 2.1 22.4 1.0
O C:HOH9042 2.3 33.3 1.0
O C:HOH9086 2.3 35.8 1.0
CD C:GLU138 2.8 26.1 1.0
OE1 C:GLU138 2.9 24.6 1.0
CE1 C:HIS102 3.0 23.8 1.0
CD2 C:HIS102 3.1 23.8 1.0
NZ C:LYS101 3.7 37.4 1.0
O C:HOH9070 3.8 36.4 1.0
CD C:LYS101 3.9 31.0 1.0
ND1 C:HIS102 4.1 23.6 1.0
CG C:HIS102 4.2 22.2 1.0
CG C:GLU138 4.3 26.3 1.0
CB C:LYS101 4.3 26.2 1.0
CE C:LYS101 4.4 33.7 1.0
CG1 C:VAL134 4.8 21.7 1.0
CG C:LYS101 4.8 28.0 1.0
O C:HOH9058 5.0 36.7 1.0
CB C:GLU138 5.0 25.7 1.0

Copper binding site 4 out of 4 in 1s1q

Go back to Copper Binding Sites List in 1s1q
Copper binding site 4 out of 4 in the TSG101(Uev) Domain in Complex with Ubiquitin


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of TSG101(Uev) Domain in Complex with Ubiquitin within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cu9004

b:40.6
occ:1.00
O D:HOH9005 2.0 38.5 1.0
OD1 D:ASP32 2.0 28.7 1.0
O D:HOH9060 2.1 33.0 1.0
O D:HOH9061 2.1 51.3 1.0
CG D:ASP32 3.1 29.2 1.0
O D:HOH9026 3.1 65.9 1.0
OD2 D:ASP32 3.4 32.3 1.0
OE1 D:GLN31 4.2 30.7 1.0
O D:ALA28 4.2 27.4 1.0
CB D:ASP32 4.4 27.8 1.0
N D:ASP32 4.7 26.4 1.0
CA D:ASP32 4.7 27.1 1.0
CD D:GLN31 4.8 27.7 1.0
CG D:GLN31 4.8 26.9 1.0

Reference:

W.I.Sundquist, H.L.Schubert, B.N.Kelly, G.C.Hill, J.M.Holton, C.P.Hill. Ubiquitin Recognition By the Human TSG101 Protein Mol.Cell V. 13 783 2004.
ISSN: ISSN 1097-2765
PubMed: 15053872
DOI: 10.1016/S1097-2765(04)00129-7
Page generated: Thu Sep 3 16:17:45 2020
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