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Nickel in PDB 1sdw: Reduced (Cu+) Peptidylglycine Alpha-Hydroxylating Monooxygenase with Bound Peptide and Dioxygen

Enzymatic activity of Reduced (Cu+) Peptidylglycine Alpha-Hydroxylating Monooxygenase with Bound Peptide and Dioxygen

All present enzymatic activity of Reduced (Cu+) Peptidylglycine Alpha-Hydroxylating Monooxygenase with Bound Peptide and Dioxygen:
1.14.17.3;

Protein crystallography data

The structure of Reduced (Cu+) Peptidylglycine Alpha-Hydroxylating Monooxygenase with Bound Peptide and Dioxygen, PDB code: 1sdw was solved by S.T.Prigge, B.A.Eipper, R.E.Mains, L.M.Amzel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.69 / 1.85
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 69.478, 68.979, 82.108, 90.00, 90.00, 90.00
R / Rfree (%) 19.7 / 22.6

Other elements in 1sdw:

The structure of Reduced (Cu+) Peptidylglycine Alpha-Hydroxylating Monooxygenase with Bound Peptide and Dioxygen also contains other interesting chemical elements:

Iodine (I) 8 atoms
Copper (Cu) 2 atoms

Nickel Binding Sites:

The binding sites of Nickel atom in the Reduced (Cu+) Peptidylglycine Alpha-Hydroxylating Monooxygenase with Bound Peptide and Dioxygen (pdb code 1sdw). This binding sites where shown within 5.0 Angstroms radius around Nickel atom.
In total only one binding site of Nickel was determined in the Reduced (Cu+) Peptidylglycine Alpha-Hydroxylating Monooxygenase with Bound Peptide and Dioxygen, PDB code: 1sdw:

Nickel binding site 1 out of 1 in 1sdw

Go back to Nickel Binding Sites List in 1sdw
Nickel binding site 1 out of 1 in the Reduced (Cu+) Peptidylglycine Alpha-Hydroxylating Monooxygenase with Bound Peptide and Dioxygen


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 1 of Reduced (Cu+) Peptidylglycine Alpha-Hydroxylating Monooxygenase with Bound Peptide and Dioxygen within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ni359

b:32.7
occ:1.00
 O A:HOH362 2.0 27.2 1.0
O2 A:GOL363 2.0 35.9 1.0
O A:HOH361 2.0 31.7 1.0
NE2 A:HIS235 2.0 29.7 1.0
O1 A:GOL363 2.3 33.6 1.0
C1 A:GOL363 2.7 43.8 1.0
C2 A:GOL363 2.8 49.0 1.0
CD2 A:HIS235 3.0 28.6 1.0
CE1 A:HIS235 3.0 28.9 1.0
C3 A:GOL363 4.1 54.2 1.0
CG A:HIS235 4.2 27.8 1.0
ND1 A:HIS235 4.2 25.7 1.0
O A:HOH454 4.2 45.9 1.0
CB A:ASP282 4.2 31.4 1.0
OD2 A:ASP282 4.3 35.5 1.0
O A:HOH471 4.3 48.7 1.0
O A:HOH427 4.5 39.3 1.0
CG A:ASP282 4.6 38.6 1.0
O3 A:GOL363 4.9 61.8 1.0

Reference:

S.T.Prigge, B.A.Eipper, R.E.Mains, L.M.Amzel. Dioxygen Binds End-on to Mononuclear Copper in A Precatalytic Enzyme Complex. Science V. 304 864 2004.
ISSN: ISSN 0036-8075
PubMed: 15131304
DOI: 10.1126/SCIENCE.1094583
Page generated: Wed Oct 9 16:25:12 2024

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