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Calcium in PDB 1gxo: Mutant D189A of Family 10 Polysaccharide Lyase From Cellvibrio Cellulosa in Complex with Trigalaturonic Acid

Enzymatic activity of Mutant D189A of Family 10 Polysaccharide Lyase From Cellvibrio Cellulosa in Complex with Trigalaturonic Acid

All present enzymatic activity of Mutant D189A of Family 10 Polysaccharide Lyase From Cellvibrio Cellulosa in Complex with Trigalaturonic Acid:
4.2.2.2;

Protein crystallography data

The structure of Mutant D189A of Family 10 Polysaccharide Lyase From Cellvibrio Cellulosa in Complex with Trigalaturonic Acid, PDB code: 1gxo was solved by S.J.Charnock, I.E.Brown, J.P.Turkenburg, G.W.Black, G.J.Davies, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 52.70 / 2.05
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 105.428, 54.917, 47.185, 90.00, 90.00, 90.00
R / Rfree (%) 17.3 / 22.8

Calcium Binding Sites:

The binding sites of Calcium atom in the Mutant D189A of Family 10 Polysaccharide Lyase From Cellvibrio Cellulosa in Complex with Trigalaturonic Acid (pdb code 1gxo). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Mutant D189A of Family 10 Polysaccharide Lyase From Cellvibrio Cellulosa in Complex with Trigalaturonic Acid, PDB code: 1gxo:

Calcium binding site 1 out of 1 in 1gxo

Go back to Calcium Binding Sites List in 1gxo
Calcium binding site 1 out of 1 in the Mutant D189A of Family 10 Polysaccharide Lyase From Cellvibrio Cellulosa in Complex with Trigalaturonic Acid


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Mutant D189A of Family 10 Polysaccharide Lyase From Cellvibrio Cellulosa in Complex with Trigalaturonic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca1652

b:47.5
occ:1.00
O A:HOH2169 2.2 22.4 1.0
O A:HOH2095 2.5 43.3 1.0
O6B A:ADA1650 2.7 28.4 1.0
OD1 A:ASP451 2.8 17.5 1.0
O6A A:ADA1651 3.0 24.5 1.0
O A:HOH2168 3.0 25.3 1.0
OD1 A:ASN390 3.3 20.5 1.0
O5 A:ADA1651 3.3 24.0 1.0
OD2 A:ASP451 3.4 19.6 1.0
CG A:ASP451 3.5 17.8 1.0
C6 A:ADA1650 3.6 27.0 1.0
NH2 A:ARG524 3.9 10.1 1.0
C6 A:ADA1651 4.0 25.5 1.0
O6A A:ADA1650 4.1 28.1 1.0
C1 A:ADA1651 4.2 23.3 1.0
C5 A:ADA1651 4.2 25.0 1.0
CG A:ASN390 4.3 18.9 1.0
C4 A:ADA1650 4.6 23.6 1.0
ND2 A:ASN390 4.7 18.1 1.0
C5 A:ADA1650 4.7 24.9 1.0
NH2 A:ARG596 4.7 18.2 1.0
O4 A:ADA1650 4.9 22.5 1.0
CZ A:ARG524 4.9 15.9 1.0
CB A:ASP451 5.0 17.1 1.0
NH1 A:ARG524 5.0 16.1 1.0

Reference:

S.J.Charnock, I.E.Brown, J.P.Turkenburg, G.W.Black, G.J.Davies. Convergent Evolution Sheds Light on the Anti-Beta-Elimination Mechanism Common to Family 1 and 10 Polysaccharide Lyases Proc.Natl.Acad.Sci.Usa V. 99 12067 2002.
ISSN: ISSN 0027-8424
PubMed: 12221284
DOI: 10.1073/PNAS.182431199
Page generated: Mon Jul 7 15:24:42 2025

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