Copper in PDB 6alv: Crystal Structure of H107A-Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) Mutant (No Cuh Bound)

All present enzymatic activity of Crystal Structure of H107A-Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) Mutant (No Cuh Bound):
1.14.17.3; 4.3.2.5;

The structure of Crystal Structure of H107A-Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) Mutant (No Cuh Bound), PDB code: 6alv 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)	50.00 / 3.50
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	69.045, 68.857, 81.532, 90.00, 90.00, 90.00
R / Rfree (%)	27.5 / 29.8

The binding sites of Copper atom in the Crystal Structure of H107A-Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) Mutant (No Cuh Bound) (pdb code 6alv). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Crystal Structure of H107A-Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) Mutant (No Cuh Bound), PDB code: 6alv:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Crystal Structure of H107A-Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) Mutant (No Cuh Bound)


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 H107A-Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) Mutant (No Cuh Bound) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu1001 b:31.5 occ:1.00 NE2 A:HIS242 2.1 26.1 1.0 NE2 A:HIS244 2.2 46.1 1.0 SD A:MET314 2.3 31.1 1.0 O A:HOH1101 2.5 1.0 1.0 CE1 A:HIS242 2.8 26.5 1.0 CE1 A:HIS244 3.0 47.3 1.0 CD2 A:HIS242 3.3 26.4 1.0 CD2 A:HIS244 3.3 45.3 1.0 CG A:MET314 3.4 32.4 1.0 CE A:MET314 3.9 30.6 1.0 ND1 A:HIS242 4.0 26.3 1.0 ND1 A:HIS244 4.1 46.0 1.0 CB A:MET314 4.2 33.5 1.0 O A:GLY308 4.2 47.7 1.0 CG A:HIS242 4.3 26.8 1.0 CG A:HIS244 4.3 44.5 1.0 CA A:GLY308 4.5 44.6 1.0 C A:GLY308 4.5 48.7 1.0 O A:GLY307 4.6 38.5 1.0

Copper binding site 2 out of 2 in the Crystal Structure of H107A-Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) Mutant (No Cuh Bound)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Crystal Structure of H107A-Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) Mutant (No Cuh Bound) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu1002 b:34.7 occ:1.00 NE2 A:HIS235 2.1 40.5 1.0 O2 A:GOL1004 2.3 32.4 1.0 N1 A:AZI1003 2.8 45.0 1.0 CD2 A:HIS235 2.9 39.2 1.0 CE1 A:HIS235 3.0 40.2 1.0 C2 A:GOL1004 3.1 32.8 1.0 C1 A:GOL1004 3.2 30.4 1.0 N2 A:AZI1003 3.3 46.1 1.0 C3 A:GOL1004 3.4 35.8 1.0 O3 A:GOL1004 3.4 38.2 1.0 CB A:ASP282 3.8 41.1 1.0 CG A:HIS235 4.0 37.7 1.0 O1 A:GOL1004 4.0 27.9 1.0 ND1 A:HIS235 4.0 38.8 1.0 N3 A:AZI1003 4.1 42.4 1.0 CG A:ASP282 4.6 41.5 1.0 OD2 A:ASP282 4.7 41.0 1.0 CA A:ASP282 4.8 42.0 1.0

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