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Copper in PDB 1yjk: Reduced Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) in A New Crystal Form

Enzymatic activity of Reduced Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) in A New Crystal Form

All present enzymatic activity of Reduced Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) in A New Crystal Form:
1.14.17.3;

Protein crystallography data

The structure of Reduced Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) in A New Crystal Form, PDB code: 1yjk was solved by X.Siebert, B.A.Eipper, R.E.Mains, S.T.Prigge, N.J.Blackburn, L.M.Amzel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.22 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 59.146, 66.335, 69.917, 90.00, 90.00, 90.00
R / Rfree (%) 19.6 / 26

Copper Binding Sites:

The binding sites of Copper atom in the Reduced Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) in A New Crystal Form (pdb code 1yjk). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Reduced Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) in A New Crystal Form, PDB code: 1yjk:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 1yjk

Go back to Copper Binding Sites List in 1yjk
Copper binding site 1 out of 2 in the Reduced Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) in A New Crystal Form


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Reduced Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) in A New Crystal Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu357

b:51.3
occ:1.00
ND1 A:HIS108 2.0 42.9 1.0
ND1 A:HIS172 2.0 40.1 1.0
ND1 A:HIS107 2.0 43.0 1.0
CE1 A:HIS107 2.8 43.6 1.0
CE1 A:HIS172 2.9 35.9 1.0
CE1 A:HIS108 2.9 42.0 1.0
CG A:HIS108 3.0 36.8 1.0
CG A:HIS107 3.1 39.9 1.0
CG A:HIS172 3.1 31.2 1.0
O A:HOH879 3.4 49.0 1.0
CB A:HIS108 3.4 31.2 1.0
CB A:HIS107 3.6 32.8 1.0
CB A:HIS172 3.6 28.9 1.0
N A:HIS108 3.7 30.5 1.0
NE2 A:HIS107 3.9 46.2 1.0
C A:HIS107 4.0 31.9 1.0
NE2 A:HIS172 4.0 35.6 1.0
NE2 A:HIS108 4.1 41.9 1.0
CD2 A:HIS107 4.1 44.7 1.0
CA A:HIS108 4.1 29.5 1.0
CD2 A:HIS108 4.1 40.6 1.0
CD2 A:HIS172 4.2 34.6 1.0
O A:HIS107 4.4 30.7 1.0
CA A:HIS107 4.4 32.6 1.0
OH A:TYR79 4.6 41.0 1.0
O A:HIS172 4.8 27.4 1.0
CA A:HIS172 5.0 26.2 1.0
C A:HIS108 5.0 28.6 1.0

Copper binding site 2 out of 2 in 1yjk

Go back to Copper Binding Sites List in 1yjk
Copper binding site 2 out of 2 in the Reduced Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) in A New Crystal Form


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Reduced Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) in A New Crystal Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu358

b:49.8
occ:1.00
O A:HOH885 2.0 49.7 1.0
NE2 A:HIS244 2.0 41.6 1.0
NE2 A:HIS242 2.1 33.3 1.0
SD A:MET314 2.2 40.9 1.0
CD2 A:HIS244 2.9 37.8 1.0
CD2 A:HIS242 3.0 31.9 1.0
CE1 A:HIS244 3.0 38.6 1.0
CE1 A:HIS242 3.1 34.2 1.0
CG A:MET314 3.2 38.6 1.0
O A:HOH882 3.6 58.1 1.0
CB A:MET314 3.9 34.1 1.0
CE A:MET314 3.9 44.8 1.0
CG A:HIS244 4.1 36.0 1.0
ND1 A:HIS244 4.1 39.3 1.0
CG A:HIS242 4.2 32.2 1.0
ND1 A:HIS242 4.2 30.1 1.0

Reference:

X.Siebert, B.A.Eipper, R.E.Mains, S.T.Prigge, N.J.Blackburn, L.M.Amzel. The Catalytic Copper of Peptidylglycine Alpha-Hydroxylating Monooxygenase Also Plays A Critical Structural Role. Biophys.J. V. 89 3312 2005.
ISSN: ISSN 0006-3495
PubMed: 16100265
DOI: 10.1529/BIOPHYSJ.105.066100
Page generated: Sun Dec 13 11:03:10 2020

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