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Copper in PDB 2hrn: Solution Structure of Cu(I) P174L-HSCO1

Copper Binding Sites:

The binding sites of Copper atom in the Solution Structure of Cu(I) P174L-HSCO1 (pdb code 2hrn). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total only one binding site of Copper was determined in the Solution Structure of Cu(I) P174L-HSCO1, PDB code: 2hrn:

Copper binding site 1 out of 1 in 2hrn

Go back to Copper Binding Sites List in 2hrn
Copper binding site 1 out of 1 in the Solution Structure of Cu(I) P174L-HSCO1


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Solution Structure of Cu(I) P174L-HSCO1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu302

b:2.1
occ:1.00
NE2 A:HIS260 2.1 1.9 1.0
SG A:CYS173 2.4 2.3 1.0
SG A:CYS169 2.4 2.9 1.0
HB2 A:HIS168 2.5 5.9 1.0
HB3 A:PHE166 2.7 2.8 1.0
H A:CYS169 2.9 2.4 1.0
CD2 A:HIS260 3.0 2.7 1.0
HB2 A:CYS169 3.1 2.5 1.0
HD2 A:HIS260 3.1 3.7 1.0
CE1 A:HIS260 3.2 2.0 1.0
H A:PHE166 3.2 2.8 1.0
H A:HIS168 3.3 3.2 1.0
CB A:CYS169 3.4 2.6 1.0
HB2 A:CYS173 3.5 1.8 1.0
HE1 A:HIS260 3.5 2.8 1.0
CB A:HIS168 3.6 5.0 1.0
CB A:CYS173 3.6 1.7 1.0
O A:PHE166 3.7 3.5 1.0
CB A:PHE166 3.7 2.9 1.0
N A:CYS169 3.7 2.3 1.0
C A:PHE166 3.9 2.7 1.0
N A:PHE166 3.9 3.0 1.0
N A:HIS168 4.0 2.8 1.0
CA A:PHE166 4.0 2.9 1.0
HB3 A:CYS173 4.0 2.1 1.0
HB3 A:HIS168 4.1 5.2 1.0
HB2 A:PHE166 4.1 3.5 1.0
HD1 A:PHE166 4.1 3.3 1.0
CG A:HIS260 4.1 2.5 1.0
CA A:HIS168 4.2 3.4 1.0
ND1 A:HIS260 4.2 2.1 1.0
CA A:CYS169 4.2 2.5 1.0
HB3 A:CYS169 4.3 3.3 1.0
C A:HIS168 4.3 2.7 1.0
H A:CYS173 4.3 1.7 1.0
CG A:HIS168 4.4 6.1 1.0
HG13 A:VAL172 4.4 2.7 1.0
N A:THR167 4.6 2.1 1.0
HD1 A:HIS168 4.6 7.6 1.0
CG A:PHE166 4.8 3.2 1.0
ND1 A:HIS168 4.8 7.3 1.0
CD1 A:PHE166 4.9 3.1 1.0
CA A:CYS173 4.9 1.5 1.0
HA A:CYS169 4.9 3.2 1.0
HA2 A:GLY165 5.0 2.4 1.0
C A:THR167 5.0 2.3 1.0

Reference:

L.Banci, I.Bertini, S.Ciofi-Baffoni, I.Leontari, M.Martinelli, P.Palumaa, R.Sillard, S.Wang. Human SCO1 Functional Studies and Pathological Implications of the P174L Mutant. Proc.Natl.Acad.Sci.Usa V. 104 15 2007.
ISSN: ISSN 0027-8424
PubMed: 17182746
DOI: 10.1073/PNAS.0606189103
Page generated: Thu Sep 3 16:41:40 2020
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