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Copper in PDB 3mlk: Reduced (Cu+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Nitrite

Enzymatic activity of Reduced (Cu+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Nitrite

All present enzymatic activity of Reduced (Cu+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Nitrite:
1.14.17.3;

Protein crystallography data

The structure of Reduced (Cu+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Nitrite, PDB code: 3mlk was solved by E.E.Chufan, B.A.Eipper, R.E.Mains, L.M.Amzel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 52.70 / 3.10
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 68.973, 69.317, 81.114, 90.00, 90.00, 90.00
R / Rfree (%) 21.6 / 28.2

Other elements in 3mlk:

The structure of Reduced (Cu+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Nitrite also contains other interesting chemical elements:

Nickel (Ni) 1 atom

Copper Binding Sites:

The binding sites of Copper atom in the Reduced (Cu+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Nitrite (pdb code 3mlk). 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 Reduced (Cu+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Nitrite, PDB code: 3mlk:

Copper binding site 1 out of 1 in 3mlk

Go back to Copper Binding Sites List in 3mlk
Copper binding site 1 out of 1 in the Reduced (Cu+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Nitrite


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Reduced (Cu+) Peptidylglycine Alpha-Hydroxylating Monooxygenase (Phm) with Bound Nitrite within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu358

b:76.5
occ:1.00
 NE2 A:HIS242 2.2 60.7 1.0
O2 A:NO21 2.2 69.0 1.0
O1 A:NO21 2.4 69.8 1.0
NE2 A:HIS244 2.5 63.9 1.0
N A:NO21 2.7 69.6 1.0
SD A:MET314 2.8 64.8 1.0
CD2 A:HIS242 2.9 59.9 1.0
CE1 A:HIS242 3.2 60.6 1.0
CD2 A:HIS244 3.3 62.6 1.0
CE1 A:HIS244 3.4 63.6 1.0
CE A:MET314 4.0 65.1 1.0
CG A:HIS242 4.1 60.2 1.0
CB A:MET314 4.2 63.8 1.0
CG A:MET314 4.2 64.1 1.0
ND1 A:HIS242 4.2 60.6 1.0
CG A:HIS244 4.5 62.2 1.0
ND1 A:HIS244 4.5 63.2 1.0

Reference:

E.E.Chufan, S.T.Prigge, X.Siebert, B.A.Eipper, R.E.Mains, L.M.Amzel. Differential Reactivity Between Two Copper Sites in Peptidylglycine Alpha-Hydroxylating Monooxygenase J.Am.Chem.Soc. V. 132 15565 2010.
ISSN: ISSN 0002-7863
PubMed: 20958070
DOI: 10.1021/JA103117R
Page generated: Mon Jul 14 02:25:57 2025

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