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Copper in PDB 3hhs: Crystal Structure of Manduca Sexta Prophenoloxidase

Enzymatic activity of Crystal Structure of Manduca Sexta Prophenoloxidase

All present enzymatic activity of Crystal Structure of Manduca Sexta Prophenoloxidase:
1.14.18.1;

Protein crystallography data

The structure of Crystal Structure of Manduca Sexta Prophenoloxidase, PDB code: 3hhs was solved by Y.Li, Y.Wang, H.Jiang, J.Deng, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.45 / 1.97
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 148.832, 153.664, 75.763, 90.00, 90.00, 90.00
R / Rfree (%) 15.4 / 19.4

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of Manduca Sexta Prophenoloxidase (pdb code 3hhs). 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 Manduca Sexta Prophenoloxidase, PDB code: 3hhs:
Jump to Copper binding site number: 1; 2; 3; 4;

Copper binding site 1 out of 4 in 3hhs

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Copper binding site 1 out of 4 in the Crystal Structure of Manduca Sexta Prophenoloxidase


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 Manduca Sexta Prophenoloxidase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu696

b:24.0
occ:1.00
 NE2 A:HIS245 2.0 11.5 1.0
NE2 A:HIS219 2.1 13.5 1.0
NE2 A:HIS215 2.1 11.5 1.0
O A:HOH759 2.7 46.7 1.0
CE1 A:HIS245 2.9 10.2 1.0
CD2 A:HIS215 3.0 10.8 1.0
CE1 A:HIS215 3.0 10.0 1.0
CE1 A:HIS219 3.0 10.7 1.0
CD2 A:HIS245 3.1 9.8 1.0
CD2 A:HIS219 3.1 9.9 1.0
OE1 A:GLU395 3.8 21.4 0.4
ND1 A:HIS245 4.0 9.3 1.0
ND1 A:HIS215 4.1 11.5 1.0
CG A:HIS215 4.1 11.3 1.0
CE A:MET244 4.1 21.0 1.0
CG A:HIS245 4.1 10.7 1.0
ND1 A:HIS219 4.2 9.5 1.0
CG A:HIS219 4.2 9.7 1.0
NE2 A:HIS408 4.6 20.6 1.0
CZ A:PHE404 4.6 12.1 1.0
CE1 A:PHE404 4.7 12.3 1.0
CE1 A:HIS408 4.7 16.1 1.0
CU A:CU697 4.9 33.5 1.0
CD A:GLU395 4.9 18.6 0.4
CE3 A:TRP218 5.0 8.3 1.0

Copper binding site 2 out of 4 in 3hhs

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Copper binding site 2 out of 4 in the Crystal Structure of Manduca Sexta Prophenoloxidase


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 Manduca Sexta Prophenoloxidase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu697

b:33.5
occ:1.00
 NE2 A:HIS372 2.1 24.3 1.0
NE2 A:HIS408 2.1 20.6 1.0
NE2 A:HIS368 2.1 19.1 1.0
O A:HOH759 2.5 46.7 1.0
CE1 A:HIS372 2.9 24.1 1.0
CD2 A:HIS408 2.9 14.6 1.0
CD2 A:HIS368 3.0 11.2 1.0
CE1 A:HIS408 3.0 16.1 1.0
CD2 A:HIS372 3.1 19.2 1.0
CE1 A:HIS368 3.2 14.9 1.0
CE1 A:PHE404 3.9 12.3 1.0
ND1 A:HIS408 4.0 14.5 1.0
CG A:HIS408 4.0 13.7 1.0
ND1 A:HIS372 4.1 23.9 1.0
CG A:HIS368 4.1 11.4 1.0
ND1 A:HIS368 4.2 14.2 1.0
CG A:HIS372 4.2 19.1 1.0
CD1 A:PHE404 4.5 11.5 1.0
CG1 A:VAL407 4.7 10.8 1.0
CZ A:PHE404 4.7 12.1 1.0
CU A:CU696 4.9 24.0 1.0

Copper binding site 3 out of 4 in 3hhs

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Copper binding site 3 out of 4 in the Crystal Structure of Manduca Sexta Prophenoloxidase


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 Manduca Sexta Prophenoloxidase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu1

b:23.8
occ:1.00
 NE2 B:HIS406 2.0 10.7 1.0
NE2 B:HIS370 2.0 18.1 1.0
NE2 B:HIS366 2.1 16.3 1.0
CE1 B:HIS406 2.9 12.3 1.0
CD2 B:HIS370 2.9 16.3 1.0
CD2 B:HIS406 3.0 11.3 1.0
CE1 B:HIS370 3.0 15.0 1.0
CD2 B:HIS366 3.1 14.3 1.0
CE1 B:HIS366 3.1 13.8 1.0
ND1 B:HIS406 4.0 13.2 1.0
CE1 B:PHE402 4.0 12.3 1.0
CG B:HIS406 4.1 12.4 1.0
CG B:HIS370 4.1 15.7 1.0
ND1 B:HIS370 4.1 15.8 1.0
ND1 B:HIS366 4.2 15.5 1.0
CG B:HIS366 4.2 15.5 1.0
CD1 B:TRP405 4.3 12.2 1.0
CD1 B:PHE402 4.5 11.0 1.0
CU B:CU686 4.5 25.8 1.0
CZ B:PHE402 4.5 14.0 1.0
NE2 B:HIS239 4.7 13.2 1.0
NE1 B:TRP405 4.8 14.3 1.0
CD2 B:HIS239 4.9 10.1 1.0

Copper binding site 4 out of 4 in 3hhs

Go back to Copper Binding Sites List in 3hhs
Copper binding site 4 out of 4 in the Crystal Structure of Manduca Sexta Prophenoloxidase


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 Manduca Sexta Prophenoloxidase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu686

b:25.8
occ:1.00
 NE2 B:HIS239 2.0 13.2 1.0
NE2 B:HIS209 2.0 15.9 1.0
NE2 B:HIS213 2.1 16.6 1.0
CE1 B:HIS239 2.8 11.4 1.0
CD2 B:HIS209 2.9 13.3 1.0
CE1 B:HIS209 3.0 13.6 1.0
CD2 B:HIS213 3.1 14.9 1.0
CE1 B:HIS213 3.1 14.5 1.0
CD2 B:HIS239 3.1 10.1 1.0
ND1 B:HIS239 4.0 8.1 1.0
CG B:HIS209 4.0 12.7 1.0
ND1 B:HIS209 4.0 14.5 1.0
CG B:HIS239 4.1 11.1 1.0
ND1 B:HIS213 4.2 13.8 1.0
CG B:HIS213 4.2 16.1 1.0
CE B:MET238 4.2 21.7 1.0
CZ B:PHE402 4.3 14.0 1.0
CE1 B:PHE402 4.5 12.3 1.0
NE2 B:HIS406 4.5 10.7 1.0
CU B:CU1 4.5 23.8 1.0
CE1 B:HIS406 4.6 12.3 1.0

Reference:

Y.Li, Y.Wang, H.Jiang, J.Deng. Crystal Structure of Manduca Sexta Prophenoloxidase Provides Insights Into the Mechanism of Type 3 Copper Enzymes. Proc.Natl.Acad.Sci.Usa V. 106 17002 2009.
ISSN: ISSN 0027-8424
PubMed: 19805072
DOI: 10.1073/PNAS.0906095106
Page generated: Wed Oct 28 14:24:07 2020
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