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Nickel in PDB 5wja: Crystal Structure of H107A Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) in Complex with Citrate

Enzymatic activity of Crystal Structure of H107A Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) in Complex with Citrate

All present enzymatic activity of Crystal Structure of H107A Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) in Complex with Citrate:
1.14.17.3; 4.3.2.5;

Protein crystallography data

The structure of Crystal Structure of H107A Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) in Complex with Citrate, PDB code: 5wja 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) 29.77 / 2.30
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 59.544, 100.613, 101.582, 90.00, 90.00, 90.00
R / Rfree (%) 19.8 / 27.3

Other elements in 5wja:

The structure of Crystal Structure of H107A Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) in Complex with Citrate also contains other interesting chemical elements:

Copper (Cu) 3 atoms

Nickel Binding Sites:

The binding sites of Nickel atom in the Crystal Structure of H107A Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) in Complex with Citrate (pdb code 5wja). 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 H107A Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) in Complex with Citrate, PDB code: 5wja:

Nickel binding site 1 out of 1 in 5wja

Go back to Nickel Binding Sites List in 5wja
Nickel binding site 1 out of 1 in the Crystal Structure of H107A Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) in Complex with Citrate


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 H107A Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) in Complex with Citrate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ni1009

b:48.0
occ:1.00
NE2 A:HIS279 2.0 37.9 1.0
CD2 A:HIS279 3.0 36.9 1.0
CE1 A:HIS279 3.0 37.8 1.0
ND1 A:HIS279 4.1 40.4 1.0
CG A:HIS279 4.1 39.4 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 08:08:59 2024

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