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Copper in PDB 1yi9: Crystal Structure Analysis of the Oxidized Form of the M314I Mutant of Peptidylglycine Alpha-Hydroxylating Monooxygenase

Enzymatic activity of Crystal Structure Analysis of the Oxidized Form of the M314I Mutant of Peptidylglycine Alpha-Hydroxylating Monooxygenase

All present enzymatic activity of Crystal Structure Analysis of the Oxidized Form of the M314I Mutant of Peptidylglycine Alpha-Hydroxylating Monooxygenase:
1.14.17.3;

Protein crystallography data

The structure of Crystal Structure Analysis of the Oxidized Form of the M314I Mutant of Peptidylglycine Alpha-Hydroxylating Monooxygenase, PDB code: 1yi9 was solved by X.Siebert, B.A.Eipper, R.E.Mains, S.T.Prigge, N.J.Blackburn, L.M.Amzel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.20 / 1.70
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 59.479, 66.458, 70.049, 90.00, 90.00, 90.00
R / Rfree (%) 20.1 / 23.3

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure Analysis of the Oxidized Form of the M314I Mutant of Peptidylglycine Alpha-Hydroxylating Monooxygenase (pdb code 1yi9). 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 Analysis of the Oxidized Form of the M314I Mutant of Peptidylglycine Alpha-Hydroxylating Monooxygenase, PDB code: 1yi9:
Jump to Copper binding site number: 1; 2; 3; 4;

Copper binding site 1 out of 4 in 1yi9

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Copper binding site 1 out of 4 in the Crystal Structure Analysis of the Oxidized Form of the M314I Mutant of Peptidylglycine Alpha-Hydroxylating Monooxygenase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Crystal Structure Analysis of the Oxidized Form of the M314I Mutant of Peptidylglycine Alpha-Hydroxylating Monooxygenase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu357

b:57.7
occ:0.40
ND1 A:HIS108 2.0 56.5 1.0
ND1 A:HIS172 2.0 47.1 1.0
CB A:HIS108 2.6 43.9 1.0
CG A:HIS108 2.6 48.3 1.0
CE1 A:HIS172 3.0 49.4 1.0
CG A:HIS172 3.0 44.1 1.0
CE1 A:HIS108 3.2 57.5 1.0
CB A:HIS172 3.4 42.2 1.0
CA A:HIS108 3.8 41.3 1.0
CD2 A:HIS108 3.9 55.6 1.0
CB A:HIS107 3.9 42.3 0.5
N A:HIS108 3.9 40.9 1.0
NE2 A:HIS172 4.0 49.0 1.0
CD2 A:HIS172 4.1 47.6 1.0
C A:HIS107 4.1 42.0 1.0
NE2 A:HIS108 4.1 56.5 1.0
OH A:TYR79 4.3 51.3 1.0
O A:HIS107 4.4 42.2 1.0
CA A:HIS107 4.6 42.9 1.0
CA A:HIS172 4.8 40.9 1.0
C A:HIS108 4.8 40.4 1.0
CZ A:TYR79 4.8 49.3 1.0
O A:HIS108 5.0 37.6 1.0

Copper binding site 2 out of 4 in 1yi9

Go back to Copper Binding Sites List in 1yi9
Copper binding site 2 out of 4 in the Crystal Structure Analysis of the Oxidized Form of the M314I Mutant of Peptidylglycine Alpha-Hydroxylating Monooxygenase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Crystal Structure Analysis of the Oxidized Form of the M314I Mutant of Peptidylglycine Alpha-Hydroxylating Monooxygenase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu360

b:69.5
occ:1.00
NE2 A:HIS279 2.0 50.6 1.0
O A:HOH833 2.1 51.6 1.0
O A:HOH715 2.2 44.9 1.0
O A:HOH832 2.2 54.3 1.0
O A:HOH778 2.4 55.9 1.0
CE1 A:HIS279 2.8 47.4 1.0
CD2 A:HIS279 3.2 44.9 1.0
OE2 A:GLU278 3.7 57.5 1.0
ND1 A:HIS279 4.0 44.6 1.0
CG A:HIS279 4.2 44.8 1.0
CG A:GLU278 4.4 50.3 1.0
CD A:GLU278 4.5 50.9 1.0

Copper binding site 3 out of 4 in 1yi9

Go back to Copper Binding Sites List in 1yi9
Copper binding site 3 out of 4 in the Crystal Structure Analysis of the Oxidized Form of the M314I Mutant of Peptidylglycine Alpha-Hydroxylating Monooxygenase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Crystal Structure Analysis of the Oxidized Form of the M314I Mutant of Peptidylglycine Alpha-Hydroxylating Monooxygenase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu361

b:80.2
occ:0.80
ND1 A:HIS245 2.0 62.2 1.0
CG A:HIS245 2.6 57.4 1.0
O A:HOH838 2.8 67.1 1.0
CB A:HIS245 2.9 56.2 1.0
CE1 A:HIS245 3.0 57.9 1.0
CG A:GLU313 3.3 60.9 1.0
CA A:HIS245 3.8 55.6 1.0
CD2 A:HIS245 3.8 59.1 1.0
O A:HOH841 3.8 68.2 1.0
NE2 A:HIS245 3.9 56.7 1.0
CD1 A:ILE214 4.1 67.2 1.0
CD A:GLU313 4.3 63.1 1.0
CB A:GLU313 4.4 57.2 1.0
N A:HIS245 4.6 56.1 1.0
OE2 A:GLU313 4.9 64.6 1.0
OE1 A:GLU313 4.9 65.5 1.0
C A:HIS245 5.0 54.7 1.0

Copper binding site 4 out of 4 in 1yi9

Go back to Copper Binding Sites List in 1yi9
Copper binding site 4 out of 4 in the Crystal Structure Analysis of the Oxidized Form of the M314I Mutant of Peptidylglycine Alpha-Hydroxylating Monooxygenase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Crystal Structure Analysis of the Oxidized Form of the M314I Mutant of Peptidylglycine Alpha-Hydroxylating Monooxygenase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu358

b:66.2
occ:0.80
O A:HOH842 1.9 59.3 1.0
NE2 A:HIS244 2.0 62.8 1.0
NE2 A:HIS242 2.1 57.7 1.0
CE1 A:HIS244 2.5 62.4 1.0
CD2 A:HIS242 3.0 55.2 1.0
CE1 A:HIS242 3.1 55.8 1.0
O A:HOH711 3.1 61.7 1.0
CD2 A:HIS244 3.2 60.7 1.0
ND1 A:HIS244 3.7 62.5 1.0
CD1 A:ILE314 3.9 55.0 1.0
CG A:HIS244 4.1 57.9 1.0
ND1 A:HIS242 4.2 53.7 1.0
CG A:HIS242 4.2 48.3 1.0
O A:HOH791 4.8 52.2 1.0

Reference:

X.Siebert, B.A.Eipper, R.E.Mains, S.T.Prigge, N.J.Blackburn, L.M.Amzel. The Catalytic Copper of Peptidylglycine Alpha-Hydroxylating Monooxygenase Also Plays A Critical Structural Role. Biophys.J. V. 89 3312 2005.
ISSN: ISSN 0006-3495
PubMed: 16100265
DOI: 10.1529/BIOPHYSJ.105.066100
Page generated: Wed Oct 28 14:18:14 2020
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