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Chlorine in PDB 6cwc: Crystal Structure of Spaa-Slh

Protein crystallography data

The structure of Crystal Structure of Spaa-Slh, PDB code: 6cwc was solved by R.J.Blackler, S.V.Evans, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.00 / 1.90
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 72.200, 72.200, 126.629, 90.00, 90.00, 120.00
R / Rfree (%) 16.2 / 21.4

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Spaa-Slh (pdb code 6cwc). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of Spaa-Slh, PDB code: 6cwc:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 6cwc

Go back to Chlorine Binding Sites List in 6cwc
Chlorine binding site 1 out of 2 in the Crystal Structure of Spaa-Slh


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 Spaa-Slh within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl302

b:22.1
occ:1.00
N A:SER166 3.2 17.5 1.0
NE2 A:GLN179 3.3 11.0 1.0
CB A:SER166 3.5 20.0 1.0
CG A:GLN179 3.7 10.0 1.0
CB A:ALA169 3.8 16.8 1.0
O A:HOH421 3.8 25.0 1.0
CA A:SER166 3.9 18.4 1.0
CA A:PHE165 4.0 15.7 1.0
CD A:GLN179 4.0 10.3 1.0
C A:PHE165 4.1 17.7 1.0
CB A:PHE165 4.1 15.5 1.0
CD1 A:PHE165 4.2 13.3 1.0
CB A:GLN179 4.6 9.4 1.0
O A:SER166 4.7 17.9 1.0
CG A:PHE165 4.7 14.2 1.0
CA A:ALA169 4.7 17.4 1.0
OG A:SER166 4.8 25.0 1.0
C A:SER166 4.8 19.4 1.0

Chlorine binding site 2 out of 2 in 6cwc

Go back to Chlorine Binding Sites List in 6cwc
Chlorine binding site 2 out of 2 in the Crystal Structure of Spaa-Slh


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Spaa-Slh within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl303

b:22.3
occ:1.00
O A:HOH425 2.9 31.6 1.0
O B:HOH477 3.1 35.6 1.0
O A:HOH471 3.2 27.7 1.0
N A:GLY56 3.2 16.9 1.0
NE2 A:GLN57 3.3 18.3 1.0
CA A:LYS54 3.5 16.0 1.0
C A:LYS54 3.6 15.1 1.0
CA A:GLY56 3.7 16.5 1.0
N A:LEU55 3.8 15.5 1.0
CG A:GLN57 3.9 18.1 1.0
CD A:GLN57 4.1 18.1 1.0
O A:LYS54 4.1 14.3 1.0
N A:GLN57 4.1 15.6 1.0
C A:GLY56 4.2 15.9 1.0
CD B:LYS172 4.2 33.8 1.0
CB A:LYS54 4.2 17.1 1.0
O A:HOH497 4.3 18.3 1.0
O B:HOH408 4.3 38.5 1.0
C A:LEU55 4.4 15.5 1.0
N A:LYS54 4.7 16.5 1.0
CA A:LEU55 4.7 15.6 1.0
CB B:LYS172 4.7 25.7 1.0
CG A:LYS54 4.7 18.9 1.0
OD1 A:ASP52 4.8 25.7 1.0
CB A:GLN57 5.0 16.5 1.0

Reference:

R.J.Blackler, A.Lopez-Guzman, F.F.Hager, B.Janesch, G.Martinz, S.M.L.Gagnon, O.Haji-Ghassemi, P.Kosma, P.Messner, C.Schaffer, S.V.Evans. Structural Basis of Cell Wall Anchoring By Slh Domains in Paenibacillus Alvei. Nat Commun V. 9 3120 2018.
ISSN: ESSN 2041-1723
PubMed: 30087354
DOI: 10.1038/S41467-018-05471-3
Page generated: Sat Jul 12 12:35:42 2025

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