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Nickel in PDB 3phm: Reduced (Cu+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm)

Enzymatic activity of Reduced (Cu+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm)

All present enzymatic activity of Reduced (Cu+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm):
1.14.17.3;

Protein crystallography data

The structure of Reduced (Cu+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm), PDB code: 3phm 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 (°) 69.519, 68.770, 82.417, 90.00, 90.00, 90.00
R / Rfree (%) 20 / 25.7

Other elements in 3phm:

The structure of Reduced (Cu+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) also contains other interesting chemical elements:

Copper (Cu) 2 atoms

Nickel Binding Sites:

The binding sites of Nickel atom in the Reduced (Cu+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) (pdb code 3phm). 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 (Phm), PDB code: 3phm:

Nickel binding site 1 out of 1 in 3phm

Go back to Nickel Binding Sites List in 3phm
Nickel binding site 1 out of 1 in the Reduced (Cu+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm)


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 (Phm) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ni359

b:35.0
occ:1.00
 N1 A:AZI361 1.9 31.6 1.0
O A:HOH706 2.0 31.6 1.0
NE2 A:HIS235 2.1 32.4 1.0
O1 A:GOL362 2.3 43.1 1.0
O2 A:GOL362 2.3 40.1 1.0
N2 A:AZI361 2.8 55.7 1.0
C1 A:GOL362 2.9 50.5 1.0
C2 A:GOL362 3.0 51.8 1.0
CD2 A:HIS235 3.1 26.6 1.0
CE1 A:HIS235 3.1 25.8 1.0
N3 A:AZI361 3.9 54.6 1.0
CB A:ASP282 4.2 34.6 1.0
ND1 A:HIS235 4.2 27.3 1.0
O A:HOH424 4.2 48.1 1.0
CG A:HIS235 4.2 30.2 1.0
OD1 A:ASP282 4.3 35.0 1.0
C3 A:GOL362 4.4 60.4 1.0
O A:HOH370 4.5 41.8 1.0
CG A:ASP282 4.6 35.9 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 17:41:15 2024

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