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Copper in PDB 1c9e: Structure of Ferrochelatase with Copper(II) N-Methylmesoporphyrin Complex Bound at the Active Site

Enzymatic activity of Structure of Ferrochelatase with Copper(II) N-Methylmesoporphyrin Complex Bound at the Active Site

All present enzymatic activity of Structure of Ferrochelatase with Copper(II) N-Methylmesoporphyrin Complex Bound at the Active Site:
4.99.1.1;

Protein crystallography data

The structure of Structure of Ferrochelatase with Copper(II) N-Methylmesoporphyrin Complex Bound at the Active Site, PDB code: 1c9e was solved by D.Lecerof, M.N.Fodje, A.Hansson, M.Hansson, S.Al-Karadaghi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.30
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 49.840, 58.560, 98.020, 90.00, 90.00, 90.00
R / Rfree (%) 18.4 / 25.5

Other elements in 1c9e:

The structure of Structure of Ferrochelatase with Copper(II) N-Methylmesoporphyrin Complex Bound at the Active Site also contains other interesting chemical elements:

Magnesium (Mg) 1 atom

Copper Binding Sites:

The binding sites of Copper atom in the Structure of Ferrochelatase with Copper(II) N-Methylmesoporphyrin Complex Bound at the Active Site (pdb code 1c9e). 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 Structure of Ferrochelatase with Copper(II) N-Methylmesoporphyrin Complex Bound at the Active Site, PDB code: 1c9e:

Copper binding site 1 out of 1 in 1c9e

Go back to Copper Binding Sites List in 1c9e
Copper binding site 1 out of 1 in the Structure of Ferrochelatase with Copper(II) N-Methylmesoporphyrin Complex Bound at the Active Site


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Structure of Ferrochelatase with Copper(II) N-Methylmesoporphyrin Complex Bound at the Active Site within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu800

b:38.0
occ:0.67
 CU A:MP1800 0.0 38.0 0.7
N2 A:MP1800 2.0 37.0 1.0
N3 A:MP1800 2.1 37.2 1.0
N4 A:MP1800 2.2 36.8 1.0
N1 A:MP1800 2.2 36.9 1.0
C1 A:MP1800 2.6 36.9 1.0
OH A:TYR13 2.8 12.7 1.0
C14 A:MP1800 3.0 36.4 1.0
C21 A:MP1800 3.0 36.6 1.0
C24 A:MP1800 3.0 36.9 1.0
C41 A:MP1800 3.1 36.9 1.0
C31 A:MP1800 3.1 37.4 1.0
C34 A:MP1800 3.1 37.5 1.0
C11 A:MP1800 3.2 36.5 1.0
C44 A:MP1800 3.3 36.7 1.0
C15 A:MP1800 3.4 36.4 1.0
C35 A:MP1800 3.5 36.9 1.0
C25 A:MP1800 3.5 37.2 1.0
CZ A:TYR13 3.7 10.9 1.0
C45 A:MP1800 3.8 36.5 1.0
O A:HOH413 3.8 20.9 1.0
C13 A:MP1800 4.2 36.3 1.0
CG2 A:ILE29 4.2 17.3 1.0
CE1 A:TYR13 4.3 13.8 1.0
C22 A:MP1800 4.3 36.4 1.0
C23 A:MP1800 4.3 36.5 1.0
C12 A:MP1800 4.3 36.3 1.0
C42 A:MP1800 4.3 36.7 1.0
C33 A:MP1800 4.4 38.1 1.0
C32 A:MP1800 4.5 37.7 1.0
C43 A:MP1800 4.5 36.5 1.0
CE2 A:TYR13 4.6 9.2 1.0
CE1 A:HIS183 4.9 22.9 1.0
CH2 A:TRP230 4.9 16.9 1.0

Reference:

D.Lecerof, M.Fodje, A.Hansson, M.Hansson, S.Al-Karadaghi. Structural and Mechanistic Basis of Porphyrin Metallation By Ferrochelatase. J.Mol.Biol. V. 297 221 2000.
ISSN: ISSN 0022-2836
PubMed: 10704318
DOI: 10.1006/JMBI.2000.3569
Page generated: Tue Jul 30 21:41:00 2024

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