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Chlorine in PDB 5c1e: Crystal Structure of the Pectin Methylesterase From Aspergillus Niger in Penultimately Deglycosylated Form (N-Acetylglucosamine Stub at ASN84)

Enzymatic activity of Crystal Structure of the Pectin Methylesterase From Aspergillus Niger in Penultimately Deglycosylated Form (N-Acetylglucosamine Stub at ASN84)

All present enzymatic activity of Crystal Structure of the Pectin Methylesterase From Aspergillus Niger in Penultimately Deglycosylated Form (N-Acetylglucosamine Stub at ASN84):
3.1.1.11;

Protein crystallography data

The structure of Crystal Structure of the Pectin Methylesterase From Aspergillus Niger in Penultimately Deglycosylated Form (N-Acetylglucosamine Stub at ASN84), PDB code: 5c1e was solved by G.B.Jameson, M.A.K.Williams, T.S.Loo, L.M.Kent, L.D.Melton, D.Mercadante, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.16 / 1.75
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 74.614, 113.543, 88.765, 90.00, 90.00, 90.00
R / Rfree (%) 17.1 / 20.2

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of the Pectin Methylesterase From Aspergillus Niger in Penultimately Deglycosylated Form (N-Acetylglucosamine Stub at ASN84) (pdb code 5c1e). 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 Pectin Methylesterase From Aspergillus Niger in Penultimately Deglycosylated Form (N-Acetylglucosamine Stub at ASN84), PDB code: 5c1e:

Chlorine binding site 1 out of 1 in 5c1e

Go back to Chlorine Binding Sites List in 5c1e
Chlorine binding site 1 out of 1 in the Crystal Structure of the Pectin Methylesterase From Aspergillus Niger in Penultimately Deglycosylated Form (N-Acetylglucosamine Stub at ASN84)


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 Pectin Methylesterase From Aspergillus Niger in Penultimately Deglycosylated Form (N-Acetylglucosamine Stub at ASN84) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl407

b:51.4
occ:1.00
 O A:HOH619 3.3 26.5 1.0
ND2 A:ASN152 3.5 18.3 1.0
NZ A:LYS173 3.6 20.6 1.0
O A:HOH772 4.2 22.2 0.5
CE A:LYS173 4.3 19.5 1.0
CG A:ASN152 4.5 17.3 1.0
OD1 A:ASN152 4.6 17.6 1.0
O A:HOH820 4.8 41.0 1.0
O A:HOH514 4.9 49.3 1.0

Reference:

L.M.Kent, T.S.Loo, L.D.Melton, D.Mercadante, M.A.Williams, G.B.Jameson. Structure and Properties of A Non-Processive, Salt-Requiring, and Acidophilic Pectin Methylesterase From Aspergillus Niger Provide Insights Into the Key Determinants of Processivity Control. J.Biol.Chem. V. 291 1289 2016.
ISSN: ESSN 1083-351X
PubMed: 26567911
DOI: 10.1074/JBC.M115.673152
Page generated: Sat Jul 12 00:37:44 2025

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