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Copper in PDB 3ow7: Crystal Structure of the Membrane Fusion Protein Cusb From Escherichia Coli.

Protein crystallography data

The structure of Crystal Structure of the Membrane Fusion Protein Cusb From Escherichia Coli., PDB code: 3ow7 was solved by C.-C.Su, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.63 / 3.78
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 84.237, 111.008, 258.867, 90.00, 90.00, 90.00
R / Rfree (%) 28 / 32.4

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of the Membrane Fusion Protein Cusb From Escherichia Coli. (pdb code 3ow7). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 4 binding sites of Copper where determined in the Crystal Structure of the Membrane Fusion Protein Cusb From Escherichia Coli., PDB code: 3ow7:
Jump to Copper binding site number: 1; 2; 3; 4;

Copper binding site 1 out of 4 in 3ow7

Go back to Copper Binding Sites List in 3ow7
Copper binding site 1 out of 4 in the Crystal Structure of the Membrane Fusion Protein Cusb From Escherichia Coli.


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Crystal Structure of the Membrane Fusion Protein Cusb From Escherichia Coli. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu414

b:1.0
occ:1.00
SD A:MET190 1.8 0.8 1.0
NE2 A:GLN162 2.5 0.4 1.0
CE A:MET190 2.8 0.2 1.0
CG A:MET190 3.1 0.5 1.0
CD A:GLN162 3.6 0.3 1.0
CB A:MET190 3.7 0.2 1.0
CB A:LEU185 3.7 0.5 1.0
CD1 A:LEU185 3.8 0.0 1.0
CG A:LEU185 4.1 0.1 1.0
CD2 A:LEU185 4.1 0.1 1.0
CB A:TRP158 4.2 1.0 1.0
CB A:GLN162 4.2 0.2 1.0
CG A:GLN162 4.2 0.7 1.0
CG A:TRP158 4.4 0.8 1.0
CG1 A:ILE195 4.5 0.7 1.0
OE1 A:GLN162 4.5 0.9 1.0
CD2 A:TRP158 4.6 0.6 1.0
CE3 A:TRP158 4.6 0.4 1.0
CD1 A:ILE195 4.8 0.6 1.0
CA A:LEU185 4.8 0.5 1.0
O A:LEU185 4.9 0.4 1.0
C A:LEU185 5.0 0.3 1.0
O A:TRP158 5.0 0.6 1.0

Copper binding site 2 out of 4 in 3ow7

Go back to Copper Binding Sites List in 3ow7
Copper binding site 2 out of 4 in the Crystal Structure of the Membrane Fusion Protein Cusb From Escherichia Coli.


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Crystal Structure of the Membrane Fusion Protein Cusb From Escherichia Coli. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu415

b:0.7
occ:1.00
NH1 A:ARG368 2.3 0.1 1.0
CZ A:ARG368 2.7 0.2 1.0
NH2 A:ARG368 2.7 0.8 1.0
SD A:MET324 2.8 0.9 1.0
CG A:MET324 2.9 0.2 1.0
CD2 A:PHE358 3.7 0.6 1.0
CE2 A:PHE358 3.8 0.5 1.0
NE A:ARG368 3.8 0.4 1.0
CG A:PHE358 4.0 0.4 1.0
CZ A:PHE358 4.0 0.2 1.0
CB A:MET324 4.2 1.0 1.0
CD1 A:PHE358 4.3 0.2 1.0
CE1 A:PHE358 4.3 0.5 1.0
CE A:MET324 4.5 0.4 1.0
OE2 A:GLU322 4.6 0.6 1.0
CD A:ARG368 4.6 0.1 1.0
CB A:PHE358 4.7 1.0 1.0

Copper binding site 3 out of 4 in 3ow7

Go back to Copper Binding Sites List in 3ow7
Copper binding site 3 out of 4 in the Crystal Structure of the Membrane Fusion Protein Cusb From Escherichia Coli.


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Crystal Structure of the Membrane Fusion Protein Cusb From Escherichia Coli. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu414

b:0.8
occ:1.00
SD B:MET324 2.8 0.4 1.0
NH1 B:ARG368 2.9 0.1 1.0
CG B:MET324 3.0 0.8 1.0
OE2 B:GLU322 3.5 0.0 1.0
CZ B:ARG368 3.6 0.4 1.0
CE2 B:PHE358 4.0 0.8 1.0
CZ B:PHE358 4.0 0.4 1.0
CG B:GLU322 4.1 0.0 1.0
CD2 B:PHE358 4.1 0.8 1.0
NH2 B:ARG368 4.2 0.2 1.0
CE1 B:PHE358 4.2 0.3 1.0
CE B:MET324 4.2 0.7 1.0
CD B:GLU322 4.2 0.8 1.0
CG B:PHE358 4.3 0.9 1.0
CD1 B:PHE358 4.3 0.3 1.0
NE B:ARG368 4.4 0.5 1.0
O B:GLU322 4.4 0.5 1.0
CB B:MET324 4.5 0.1 1.0
O A:TRP256 5.0 0.7 1.0

Copper binding site 4 out of 4 in 3ow7

Go back to Copper Binding Sites List in 3ow7
Copper binding site 4 out of 4 in the Crystal Structure of the Membrane Fusion Protein Cusb From Escherichia Coli.


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Crystal Structure of the Membrane Fusion Protein Cusb From Escherichia Coli. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu415

b:0.4
occ:1.01
NE2 B:GLN162 2.1 0.3 1.0
SD B:MET190 2.4 0.6 1.0
CE2 B:PHE208 2.8 0.7 1.0
CE B:MET190 2.9 0.8 1.0
CD B:GLN162 3.0 0.3 1.0
OE1 B:GLN162 3.1 0.6 1.0
CD1 B:TRP158 3.5 0.3 1.0
CZ B:PHE208 3.7 0.9 1.0
CG B:MET190 3.7 0.9 1.0
NE1 B:TRP158 3.8 0.2 1.0
CD2 B:PHE208 3.8 1.0 1.0
CB B:GLN205 4.1 0.1 1.0
O B:GLN205 4.2 0.2 1.0
CG B:GLN162 4.4 0.3 1.0
CB B:MET190 4.4 0.4 1.0
CD2 B:LEU185 4.4 0.8 1.0
CG B:TRP158 4.8 0.6 1.0
C B:GLN205 5.0 0.8 1.0
CE1 B:PHE208 5.0 0.5 1.0

Reference:

C.C.Su, F.Yang, F.Long, D.Reyon, M.D.Routh, D.W.Kuo, A.K.Mokhtari, J.D.Van Ornam, K.L.Rabe, J.A.Hoy, Y.J.Lee, K.R.Rajashankar, E.W.Yu. Crystal Structure of the Membrane Fusion Protein Cusb From Escherichia Coli. J.Mol.Biol. V. 393 342 2009.
ISSN: ISSN 0022-2836
PubMed: 19695261
DOI: 10.1016/J.JMB.2009.08.029
Page generated: Fri Sep 4 08:13:24 2020
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