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Chlorine in PDB 6fhj: Structural Dynamics and Catalytic Properties of A Multi-Modular Xanthanase, Native.

Protein crystallography data

The structure of Structural Dynamics and Catalytic Properties of A Multi-Modular Xanthanase, Native., PDB code: 6fhj was solved by O.V.Moroz, P.F.Jensen, S.P.Mcdonald, N.Mcgregor, E.Blagova, G.Comamala, D.R.Segura, L.Anderson, S.M.Vasu, V.P.Rao, L.Giger, R.N.Monrad, A.Svendsen, J.E.Nielsen, B.Henrissat, G.J.Davies, H.Brumer, K.Rand, K.S.Wilson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 27.50 / 2.04
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 103.350, 103.350, 212.500, 90.00, 90.00, 120.00
R / Rfree (%) 18 / 21

Other elements in 6fhj:

The structure of Structural Dynamics and Catalytic Properties of A Multi-Modular Xanthanase, Native. also contains other interesting chemical elements:

Calcium (Ca) 5 atoms
Sodium (Na) 3 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structural Dynamics and Catalytic Properties of A Multi-Modular Xanthanase, Native. (pdb code 6fhj). 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 Structural Dynamics and Catalytic Properties of A Multi-Modular Xanthanase, Native., PDB code: 6fhj:

Chlorine binding site 1 out of 1 in 6fhj

Go back to Chlorine Binding Sites List in 6fhj
Chlorine binding site 1 out of 1 in the Structural Dynamics and Catalytic Properties of A Multi-Modular Xanthanase, Native.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structural Dynamics and Catalytic Properties of A Multi-Modular Xanthanase, Native. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl2409

b:39.7
occ:1.00
OG1 A:THR409 2.5 21.7 1.0
O A:VAL413 2.7 20.3 1.0
O A:MET406 2.8 22.4 1.0
N A:VAL413 3.0 22.4 1.0
O A:THR409 3.2 22.6 1.0
CB A:THR409 3.3 22.3 1.0
N A:THR409 3.4 22.4 1.0
CG2 A:THR409 3.5 22.1 1.0
N A:GLY412 3.5 23.3 1.0
C A:MET406 3.5 22.6 1.0
C A:VAL413 3.6 20.7 1.0
CA A:THR409 3.7 22.7 1.0
C A:THR409 3.7 23.4 1.0
CA A:MET406 3.7 23.0 1.0
C A:GLY412 3.8 22.8 1.0
O A:HOH2573 3.8 29.5 1.0
CA A:VAL413 3.8 21.2 1.0
CA A:GLY412 3.8 23.5 1.0
CG1 A:VAL413 3.8 22.0 1.0
CB A:MET406 4.3 25.2 1.0
CB A:VAL413 4.4 21.9 1.0
N A:TYR411 4.4 23.1 1.0
C A:TYR411 4.5 23.0 1.0
O A:LEU405 4.5 20.7 1.0
C A:GLU408 4.6 22.8 1.0
N A:GLU408 4.6 22.1 1.0
N A:PRO410 4.7 24.7 1.0
CG A:MET406 4.8 27.9 1.0
N A:ASP407 4.8 22.2 1.0
O A:GLY412 4.8 22.9 1.0
N A:LEU414 4.9 19.7 1.0
N A:MET406 4.9 21.7 1.0
CA A:TYR411 4.9 22.9 1.0

Reference:

O.V.Moroz, P.F.Jensen, S.P.Mcdonald, N.Mcgregor, E.Blagova, G.Comamala, D.R.Segura, L.Anderson, S.M.Vasu, V.P.Rao, L.Giger, R.N.Monrad, A.Svendsen, J.E.Nielsen, B.Henrissat, G.J.Davies, H.Brumer, K.Rand, K.S.Wilson. Structural Dynamics and Catalytic Properties of A Multimodular Xanthanase Acs Catalysis 2018.
ISSN: ESSN 2155-5435
DOI: 10.1021/ACSCATAL.8B00666
Page generated: Sat Jul 12 14:02:11 2025

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