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Chlorine in PDB 1pf3: Crystal Structure of the M441L Mutant of the Multicopper Oxidase Cueo

Protein crystallography data

The structure of Crystal Structure of the M441L Mutant of the Multicopper Oxidase Cueo, PDB code: 1pf3 was solved by S.A.Roberts, G.F.Wildner, G.Grass, A.Weichsel, A.Ambrus, C.Rensing, W.R.Montfort, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.50
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 50.445, 91.193, 53.905, 90.00, 102.35, 90.00
R / Rfree (%) 19.1 / 22.8

Other elements in 1pf3:

The structure of Crystal Structure of the M441L Mutant of the Multicopper Oxidase Cueo also contains other interesting chemical elements:

Copper (Cu) 4 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of the M441L Mutant of the Multicopper Oxidase Cueo (pdb code 1pf3). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of the M441L Mutant of the Multicopper Oxidase Cueo, PDB code: 1pf3:

Chlorine binding site 1 out of 1 in 1pf3

Go back to Chlorine Binding Sites List in 1pf3
Chlorine binding site 1 out of 1 in the Crystal Structure of the M441L Mutant of the Multicopper Oxidase Cueo


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of the M441L Mutant of the Multicopper Oxidase Cueo within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl702

b:24.0
occ:1.00
CL A:C2C702 0.0 24.0 1.0
CU2 A:C2C702 2.4 16.1 1.0
CU3 A:C2C702 2.5 13.8 1.0
O A:HOH2324 2.9 26.3 1.0
NE2 A:HIS501 3.2 11.1 1.0
NE2 A:HIS141 3.2 11.1 1.0
NE2 A:HIS499 3.3 12.2 1.0
CU A:CU703 3.3 17.0 0.8
CE1 A:HIS141 3.3 9.9 1.0
NE2 A:HIS143 3.4 16.9 1.0
CD2 A:HIS501 3.4 11.2 1.0
CE1 A:HIS499 3.5 13.4 1.0
CD2 A:HIS101 3.5 10.2 1.0
CD2 A:HIS446 3.5 11.9 1.0
ND1 A:HIS103 3.7 9.5 1.0
NE2 A:HIS101 3.8 12.5 1.0
NE2 A:HIS448 3.8 11.5 1.0
NE2 A:HIS446 3.8 11.9 1.0
CD2 A:HIS143 3.8 13.6 1.0
CE1 A:HIS501 4.3 12.5 1.0
CE1 A:HIS103 4.3 10.2 1.0
CE1 A:HIS143 4.4 15.6 1.0
CG A:HIS103 4.5 8.7 1.0
CD2 A:HIS141 4.6 9.5 1.0
CD2 A:HIS448 4.6 11.7 1.0
CE1 A:HIS448 4.6 12.6 1.0
CG A:HIS446 4.6 12.3 1.0
CD2 A:HIS499 4.6 11.1 1.0
ND1 A:HIS141 4.6 12.9 1.0
CG A:HIS501 4.6 10.6 1.0
CG A:HIS101 4.6 10.8 1.0
ND1 A:HIS499 4.8 11.5 1.0
CB A:HIS103 4.8 8.5 1.0
CE1 A:HIS101 4.9 13.1 1.0
CG A:HIS143 5.0 13.9 1.0
CE1 A:HIS446 5.0 11.8 1.0

Reference:

S.A.Roberts, G.F.Wildner, G.Grass, A.Weichsel, A.Ambrus, C.Rensing, W.R.Montfort. A Labile Regulatory Copper Ion Lies Near the T1 Copper Site in the Multicopper Oxidase Cueo. J.Biol.Chem. V. 278 31958 2003.
ISSN: ISSN 0021-9258
PubMed: 12794077
DOI: 10.1074/JBC.M302963200
Page generated: Sat Jul 20 01:11:10 2024

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