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Nickel in PDB 1opm: Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Substrate

Enzymatic activity of Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Substrate

All present enzymatic activity of Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Substrate:
1.14.17.3;

Protein crystallography data

The structure of Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Substrate, PDB code: 1opm was solved by S.T.Prigge, L.M.Amzel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 2.10
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 69.399, 68.840, 81.047, 90.00, 90.00, 90.00
R / Rfree (%) 20 / 25.9

Other elements in 1opm:

The structure of Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Substrate also contains other interesting chemical elements:

Iodine (I) 4 atoms
Copper (Cu) 2 atoms

Nickel Binding Sites:

The binding sites of Nickel atom in the Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Substrate (pdb code 1opm). 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 Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Substrate, PDB code: 1opm:

Nickel binding site 1 out of 1 in 1opm

Go back to Nickel Binding Sites List in 1opm
Nickel binding site 1 out of 1 in the Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Substrate


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 1 of Oxidized (CU2+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Substrate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ni359

b:31.3
occ:1.00
 N1 A:AZI361 2.0 33.6 1.0
O A:HOH804 2.0 25.4 1.0
O1 A:GOL362 2.0 42.4 1.0
O2 A:GOL362 2.2 34.4 1.0
NE2 A:HIS235 2.2 27.0 1.0
N2 A:AZI361 2.8 51.0 1.0
C1 A:GOL362 2.9 48.4 1.0
C2 A:GOL362 2.9 52.2 1.0
CD2 A:HIS235 2.9 23.5 1.0
CE1 A:HIS235 3.3 27.3 1.0
N3 A:AZI361 4.0 44.5 1.0
CG A:HIS235 4.2 28.4 1.0
OD1 A:ASP282 4.2 33.9 1.0
CB A:ASP282 4.2 30.4 1.0
C3 A:GOL362 4.3 57.2 1.0
ND1 A:HIS235 4.3 26.9 1.0
O A:HOH370 4.3 42.0 1.0
O A:HOH424 4.4 39.2 1.0
CG A:ASP282 4.5 32.0 1.0
O3 A:GOL362 5.0 71.5 1.0

Reference:

S.T.Prigge, A.S.Kolhekar, B.A.Eipper, R.E.Mains, L.M.Amzel. Substrate-Mediated Electron Transfer in Peptidylglycine Alpha-Hydroxylating Monooxygenase. Nat.Struct.Biol. V. 6 976 1999.
ISSN: ISSN 1072-8368
PubMed: 10504734
DOI: 10.1038/13351
Page generated: Wed Oct 9 15:04:18 2024

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