Atomistry » Chlorine » PDB 4yvp-4z6p » 4yzx
Atomistry »
  Chlorine »
    PDB 4yvp-4z6p »
      4yzx »

Chlorine in PDB 4yzx: C. Bescii Family 3 Pectate Lyase Double Mutant K108A/D107N in Complex with Trigalacturonic Acid

Enzymatic activity of C. Bescii Family 3 Pectate Lyase Double Mutant K108A/D107N in Complex with Trigalacturonic Acid

All present enzymatic activity of C. Bescii Family 3 Pectate Lyase Double Mutant K108A/D107N in Complex with Trigalacturonic Acid:
4.2.2.2;

Protein crystallography data

The structure of C. Bescii Family 3 Pectate Lyase Double Mutant K108A/D107N in Complex with Trigalacturonic Acid, PDB code: 4yzx was solved by P.M.Alahuhta, V.V.Lunin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 34.58 / 1.25
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 138.334, 36.352, 100.106, 90.00, 132.67, 90.00
R / Rfree (%) 11 / 15.6

Other elements in 4yzx:

The structure of C. Bescii Family 3 Pectate Lyase Double Mutant K108A/D107N in Complex with Trigalacturonic Acid also contains other interesting chemical elements:

Calcium (Ca) 8 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the C. Bescii Family 3 Pectate Lyase Double Mutant K108A/D107N in Complex with Trigalacturonic Acid (pdb code 4yzx). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the C. Bescii Family 3 Pectate Lyase Double Mutant K108A/D107N in Complex with Trigalacturonic Acid, PDB code: 4yzx:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 4yzx

Go back to Chlorine Binding Sites List in 4yzx
Chlorine binding site 1 out of 2 in the C. Bescii Family 3 Pectate Lyase Double Mutant K108A/D107N in Complex with Trigalacturonic Acid


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of C. Bescii Family 3 Pectate Lyase Double Mutant K108A/D107N in Complex with Trigalacturonic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl210

b:16.4
occ:0.77
O A:HOH369 2.9 29.6 0.7
OG A:SER156 2.9 25.2 0.5
ND2 A:ASN107 3.1 15.3 1.0
NZ A:LYS130 3.2 17.1 1.0
O A:HOH341 3.2 34.2 0.8
CB A:SER156 3.5 17.4 0.5
CA A:GLY129 3.5 11.3 1.0
CB A:SER156 3.7 11.7 0.5
C A:GLY129 3.7 10.0 1.0
CG A:LYS130 3.8 12.7 1.0
CA A:ASN107 3.9 10.9 1.0
O A:GLY129 4.1 10.5 1.0
CG A:ASN107 4.1 14.6 1.0
N A:LYS130 4.1 9.5 1.0
CE A:LYS130 4.2 16.0 1.0
OG A:SER156 4.2 15.1 0.5
C A:ASN107 4.3 10.0 1.0
O A:ASN107 4.3 10.8 1.0
O A:ALA106 4.4 14.1 1.0
CD A:LYS130 4.4 13.7 1.0
CB A:ASN107 4.5 13.2 1.0
O A:HOH398 4.6 29.8 0.7
C1 A:ADA211 4.6 23.9 1.0
O5 A:ADA211 4.7 18.8 1.0
CB A:LYS130 4.8 11.8 1.0
O A:HOH383 4.8 16.9 0.9
N A:GLY129 4.8 9.7 1.0
CA A:SER156 4.8 13.1 0.5
O A:HOH400 4.9 21.0 0.7
O1 A:ADA211 4.9 27.3 1.0
N A:SER156 4.9 12.4 0.5
CA A:SER156 5.0 12.8 0.5

Chlorine binding site 2 out of 2 in 4yzx

Go back to Chlorine Binding Sites List in 4yzx
Chlorine binding site 2 out of 2 in the C. Bescii Family 3 Pectate Lyase Double Mutant K108A/D107N in Complex with Trigalacturonic Acid


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of C. Bescii Family 3 Pectate Lyase Double Mutant K108A/D107N in Complex with Trigalacturonic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl208

b:14.9
occ:0.97
OG B:SER156 3.0 20.1 0.5
O B:HOH344 3.0 19.7 0.5
ND2 B:ASN107 3.1 16.5 1.0
NZ B:LYS130 3.2 14.8 1.0
O B:HOH314 3.2 23.6 0.6
O B:HOH459 3.3 27.4 0.6
O1 B:GTR212 3.5 23.1 0.3
CB B:SER156 3.5 16.5 0.5
CA B:GLY129 3.6 9.2 1.0
CB B:SER156 3.6 10.9 0.5
C B:GLY129 3.7 9.5 1.0
CG B:LYS130 3.9 10.9 1.0
CA B:ASN107 3.9 10.3 1.0
O B:GLY129 4.1 10.7 1.0
N B:LYS130 4.1 8.6 1.0
OG B:SER156 4.1 15.8 0.5
CG B:ASN107 4.2 16.0 1.0
C B:ASN107 4.3 9.5 1.0
CE B:LYS130 4.3 13.7 1.0
O B:ASN107 4.3 10.6 1.0
O B:ALA106 4.4 12.4 1.0
CD B:LYS130 4.4 12.1 1.0
CB B:ASN107 4.5 12.3 1.0
C1 B:ADA209 4.5 14.1 0.7
O5 B:ADA209 4.6 14.8 0.7
C1 B:GTR212 4.7 25.8 0.3
O5 B:GTR212 4.7 28.1 0.3
CB B:LYS130 4.7 10.8 1.0
O1 B:ADA209 4.7 17.0 0.7
O B:HOH379 4.8 15.4 1.0
O B:HOH425 4.8 16.7 0.5
CA B:SER156 4.8 11.6 0.5
N B:GLY129 4.8 9.1 1.0
CA B:SER156 4.9 11.3 0.5
N B:SER156 4.9 10.2 0.5
N B:ASN107 4.9 10.3 1.0
O B:HOH418 5.0 28.3 1.0
CA B:LYS130 5.0 9.0 1.0

Reference:

M.Alahuhta, L.E.Taylor, R.Brunecky, D.W.Sammond, W.Michener, M.W.Adams, M.E.Himmel, Y.J.Bomble, V.Lunin. The Catalytic Mechanism and Unique Low pH Optimum of Caldicellulosiruptor Bescii Family 3 Pectate Lyase. Acta Crystallogr.,Sect.D V. 71 1946 2015.
ISSN: ESSN 1399-0047
PubMed: 26327384
DOI: 10.1107/S1399004715013760
Page generated: Sat Dec 12 11:26:38 2020

Last articles

Zn in 7VD8
Zn in 7V1R
Zn in 7V1Q
Zn in 7VPF
Zn in 7T85
Zn in 7T5F
Zn in 7NF9
Zn in 7M4M
Zn in 7M4O
Zn in 7M4N
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy