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Chlorine in PDB 1r76: Structure of A Pectate Lyase From Azospirillum Irakense

Enzymatic activity of Structure of A Pectate Lyase From Azospirillum Irakense

All present enzymatic activity of Structure of A Pectate Lyase From Azospirillum Irakense:
4.2.2.2;

Protein crystallography data

The structure of Structure of A Pectate Lyase From Azospirillum Irakense, PDB code: 1r76 was solved by H.Novoa De Armas, C.Verboven, C.De Ranter, J.Desair, A.Vande Broek, J.Vanderleyden, A.Rabijns, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 21.75 / 2.65
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 85.374, 85.374, 231.317, 90.00, 90.00, 120.00
R / Rfree (%) 19.8 / 26.2

Other elements in 1r76:

The structure of Structure of A Pectate Lyase From Azospirillum Irakense also contains other interesting chemical elements:

Mercury (Hg) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structure of A Pectate Lyase From Azospirillum Irakense (pdb code 1r76). 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 Structure of A Pectate Lyase From Azospirillum Irakense, PDB code: 1r76:

Chlorine binding site 1 out of 1 in 1r76

Go back to Chlorine Binding Sites List in 1r76
Chlorine binding site 1 out of 1 in the Structure of A Pectate Lyase From Azospirillum Irakense


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of A Pectate Lyase From Azospirillum Irakense within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl5000

b:59.1
occ:1.00
NH1 A:ARG253 3.6 20.0 1.0
NH2 A:ARG253 3.7 19.6 1.0
CZ A:ARG253 4.1 18.0 1.0

Reference:

H.Novoa De Armas, C.Verboven, C.De Ranter, J.Desair, A.Vande Broek, J.Vanderleyden, A.Rabijns. Azospirillum Irakense Pectate Lyase Displays A Toroidal Fold. Acta Crystallogr.,Sect.D V. 60 999 2004.
ISSN: ISSN 0907-4449
PubMed: 15159558
DOI: 10.1107/S090744490400602X
Page generated: Sat Dec 12 08:47:54 2020

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