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Atomistry » Copper » PDB 5zpo-6ff2 » 6an3 » |
Copper in PDB 6an3: Crystal Structure of H172A-Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) Mutant Soaked with Peptide (No Cuh Bound, No Peptide Bound)Enzymatic activity of Crystal Structure of H172A-Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) Mutant Soaked with Peptide (No Cuh Bound, No Peptide Bound)
All present enzymatic activity of Crystal Structure of H172A-Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) Mutant Soaked with Peptide (No Cuh Bound, No Peptide Bound):
1.14.17.3; 4.3.2.5; Protein crystallography data
The structure of Crystal Structure of H172A-Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) Mutant Soaked with Peptide (No Cuh Bound, No Peptide Bound), PDB code: 6an3
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:
Copper Binding Sites:
The binding sites of Copper atom in the Crystal Structure of H172A-Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) Mutant Soaked with Peptide (No Cuh Bound, No Peptide Bound)
(pdb code 6an3). This binding sites where shown within
5.0 Angstroms radius around Copper atom.
In total only one binding site of Copper was determined in the Crystal Structure of H172A-Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) Mutant Soaked with Peptide (No Cuh Bound, No Peptide Bound), PDB code: 6an3: Copper binding site 1 out of 1 in 6an3Go back to Copper Binding Sites List in 6an3
Copper binding site 1 out
of 1 in the Crystal Structure of H172A-Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) Mutant Soaked with Peptide (No Cuh Bound, No Peptide Bound)
Mono view Stereo pair view
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.
Page generated: Sun Dec 13 11:22:01 2020
ISSN: ESSN 2399-3642 PubMed: 30271955 DOI: 10.1038/S42003-018-0082-Y |
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