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Nickel in PDB 6ao6: Crystal Structure of H108A Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm)

Enzymatic activity of Crystal Structure of H108A Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm)

All present enzymatic activity of Crystal Structure of H108A Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm):
1.14.17.3;

Protein crystallography data

The structure of Crystal Structure of H108A Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm), PDB code: 6ao6 was solved by S.Maheshwari, K.Rudzka, S.B.Gabelli, L.M.Amzel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 53.17 / 2.98
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 69.123, 69.845, 81.992, 90.00, 90.00, 90.00
R / Rfree (%) 18 / 26.1

Other elements in 6ao6:

The structure of Crystal Structure of H108A Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) also contains other interesting chemical elements:

Copper (Cu) 1 atom

Nickel Binding Sites:

The binding sites of Nickel atom in the Crystal Structure of H108A Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) (pdb code 6ao6). 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 Crystal Structure of H108A Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm), PDB code: 6ao6:

Nickel binding site 1 out of 1 in 6ao6

Go back to Nickel Binding Sites List in 6ao6
Nickel binding site 1 out of 1 in the Crystal Structure of H108A 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 Crystal Structure of H108A Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ni402

b:77.1
occ:1.00
 O A:HOH503 1.7 49.9 1.0
NE2 A:HIS235 2.4 60.8 1.0
CD2 A:HIS235 3.0 58.9 1.0
CE1 A:HIS235 3.6 61.1 1.0
CB A:ASP282 3.6 78.6 1.0
CG A:ASP282 4.0 89.2 1.0
OD1 A:ASP282 4.0 89.8 1.0
CG A:HIS235 4.3 59.7 1.0
N A:ASP282 4.5 65.3 1.0
ND1 A:HIS235 4.5 60.5 1.0
CA A:ASP282 4.5 69.8 1.0
OD2 A:ASP282 4.9 0.6 1.0

Reference:

S.Maheshwari, C.Shimokawa, K.Rudzka, C.D.Kline, B.A.Eipper, R.E.Mains, S.B.Gabelli, N.Blackburn, L.M.Amzel. Effects of Copper Occupancy on the Conformational Landscape of Peptidylglycine Alpha-Hydroxylating Monooxygenase. Commun Biol V. 1 74 2018.
ISSN: ESSN 2399-3642
PubMed: 30271955
DOI: 10.1038/S42003-018-0082-Y
Page generated: Thu Oct 10 08:17:47 2024

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