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Copper in PDB 1phm: Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) From Rat

Enzymatic activity of Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) From Rat

All present enzymatic activity of Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) From Rat:
1.14.17.3;

Protein crystallography data

The structure of Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) From Rat, PDB code: 1phm was solved by S.T.Prigge, L.M.Amzel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 6.00 / 1.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 68.400, 68.660, 81.380, 90.00, 90.00, 90.00
R / Rfree (%) 19.6 / 26.1

Copper Binding Sites:

The binding sites of Copper atom in the Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) From Rat (pdb code 1phm). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 3 binding sites of Copper where determined in the Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) From Rat, PDB code: 1phm:
Jump to Copper binding site number: 1; 2; 3;

Copper binding site 1 out of 3 in 1phm

Go back to Copper Binding Sites List in 1phm
Copper binding site 1 out of 3 in the Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) From Rat


Mono view


Stereo pair view

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

b:52.1
occ:1.00
ND1 A:HIS107 1.9 59.6 1.0
ND1 A:HIS108 1.9 40.6 1.0
ND1 A:HIS172 2.3 59.4 1.0
CG A:HIS108 2.9 35.6 1.0
CG A:HIS107 2.9 57.7 1.0
CE1 A:HIS108 2.9 36.5 1.0
CE1 A:HIS107 2.9 60.6 1.0
CE1 A:HIS172 3.2 59.2 1.0
CB A:HIS107 3.3 50.5 1.0
CB A:HIS108 3.3 38.6 1.0
CG A:HIS172 3.4 58.9 1.0
N A:HIS108 3.5 42.4 1.0
C A:HIS107 3.7 46.4 1.0
CB A:HIS172 3.8 49.8 1.0
CA A:HIS108 4.0 38.9 1.0
O A:HOH438 4.0 53.8 1.0
NE2 A:HIS108 4.1 39.3 1.0
CD2 A:HIS108 4.1 35.8 1.0
NE2 A:HIS107 4.1 62.3 1.0
CD2 A:HIS107 4.1 58.9 1.0
CA A:HIS107 4.1 47.8 1.0
O A:HIS107 4.1 46.5 1.0
NE2 A:HIS172 4.4 62.8 1.0
CD2 A:HIS172 4.5 60.7 1.0
OH A:TYR79 4.7 55.3 1.0
C A:HIS108 4.9 38.7 1.0
O A:HOH588 4.9 72.1 1.0
O A:HIS108 4.9 39.5 1.0

Copper binding site 2 out of 3 in 1phm

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Copper binding site 2 out of 3 in the Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) From Rat


Mono view


Stereo pair view

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

b:35.2
occ:1.00
NE2 A:HIS242 1.9 27.9 1.0
NE2 A:HIS244 2.1 27.1 1.0
O A:HOH360 2.3 48.7 1.0
SD A:MET314 2.4 32.9 1.0
CE1 A:HIS242 2.9 26.4 1.0
CD2 A:HIS242 2.9 28.6 1.0
CD2 A:HIS244 3.0 23.8 1.0
CE1 A:HIS244 3.1 24.8 1.0
CG A:MET314 3.3 28.4 1.0
CE A:MET314 3.6 34.7 1.0
CB A:MET314 3.7 27.8 1.0
ND1 A:HIS242 4.1 29.1 1.0
CG A:HIS242 4.1 28.5 1.0
CG A:HIS244 4.2 25.7 1.0
ND1 A:HIS244 4.2 26.5 1.0
O A:HOH594 4.5 53.0 1.0
O A:GLY307 4.9 33.7 1.0

Copper binding site 3 out of 3 in 1phm

Go back to Copper Binding Sites List in 1phm
Copper binding site 3 out of 3 in the Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) From Rat


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) From Rat within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu359

b:34.1
occ:1.00
N1 A:AZI361 1.8 36.1 1.0
O A:HOH363 2.0 30.2 1.0
NE2 A:HIS235 2.1 30.7 1.0
O1 A:GOL362 2.3 42.4 1.0
O2 A:GOL362 2.3 51.2 1.0
C1 A:GOL362 2.8 50.2 1.0
N2 A:AZI361 2.8 52.3 1.0
C2 A:GOL362 2.9 57.1 1.0
CD2 A:HIS235 2.9 28.6 1.0
CE1 A:HIS235 3.2 31.4 1.0
N3 A:AZI361 4.0 50.4 1.0
CB A:ASP282 4.1 33.1 1.0
CG A:HIS235 4.1 32.8 1.0
ND1 A:HIS235 4.2 31.6 1.0
C3 A:GOL362 4.3 64.2 1.0
OD1 A:ASP282 4.4 33.0 1.0
O A:HOH424 4.5 44.0 1.0
O A:HOH370 4.5 43.6 1.0
CG A:ASP282 4.5 37.4 1.0
O A:HOH525 4.6 65.7 1.0

Reference:

S.T.Prigge, A.S.Kolhekar, B.A.Eipper, R.E.Mains, L.M.Amzel. Amidation of Bioactive Peptides: the Structure of Peptidylglycine Alpha-Hydroxylating Monooxygenase. Science V. 278 1300 1997.
ISSN: ISSN 0036-8075
PubMed: 9360928
DOI: 10.1126/SCIENCE.278.5341.1300
Page generated: Sun Dec 13 11:01:19 2020

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