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Copper in PDB 6ay0: Crystal Structure of H108A Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) Soaked with Peptide

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

All present enzymatic activity of Crystal Structure of H108A Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) Soaked with Peptide:
1.14.17.3; 4.3.2.5;

Protein crystallography data

The structure of Crystal Structure of H108A Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) Soaked with Peptide, PDB code: 6ay0 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) 48.30 / 2.60
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 58.808, 66.532, 70.217, 90.00, 90.00, 90.00
R / Rfree (%) 19.2 / 26.6

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of H108A Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) Soaked with Peptide (pdb code 6ay0). 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 H108A Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) Soaked with Peptide, PDB code: 6ay0:

Copper binding site 1 out of 1 in 6ay0

Go back to Copper Binding Sites List in 6ay0
Copper binding site 1 out of 1 in the Crystal Structure of H108A Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) Soaked with Peptide


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Crystal Structure of H108A Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) Soaked with Peptide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1001

b:67.5
occ:1.00
 NE2 A:HIS242 2.3 34.1 1.0
NE2 A:HIS244 2.5 50.5 1.0
SD A:MET314 2.5 56.1 1.0
CD2 A:HIS242 3.1 33.6 1.0
O A:HOH1141 3.1 34.8 1.0
CD2 A:HIS244 3.2 47.8 1.0
CE1 A:HIS242 3.4 35.8 1.0
CE1 A:HIS244 3.5 49.8 1.0
CG A:MET314 3.6 48.0 1.0
CE A:MET314 4.0 58.1 1.0
CB A:MET314 4.2 42.8 1.0
CG A:HIS242 4.3 33.4 1.0
ND1 A:HIS242 4.5 35.6 1.0
CG A:HIS244 4.5 48.0 1.0
ND1 A:HIS244 4.6 53.2 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: Mon Jul 14 05:54:37 2025

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