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Chlorine in PDB 2x7i: Crystal Structure of Mevalonate Kinase From Methicillin- Resistant Staphylococcus Aureus MRSA252

Protein crystallography data

The structure of Crystal Structure of Mevalonate Kinase From Methicillin- Resistant Staphylococcus Aureus MRSA252, PDB code: 2x7i was solved by M.Oke, X.Yan, L.G.Carter, K.A.Johnson, H.Liu, S.A.Mcmahon, M.F.White, J.H.Naismith, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 81.92 / 2.20
Space group P 62 2 2
Cell size a, b, c (Å), α, β, γ (°) 94.589, 94.589, 169.010, 90.00, 90.00, 120.00
R / Rfree (%) 21.105 / 25.73

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Mevalonate Kinase From Methicillin- Resistant Staphylococcus Aureus MRSA252 (pdb code 2x7i). 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 Crystal Structure of Mevalonate Kinase From Methicillin- Resistant Staphylococcus Aureus MRSA252, PDB code: 2x7i:

Chlorine binding site 1 out of 1 in 2x7i

Go back to Chlorine Binding Sites List in 2x7i
Chlorine binding site 1 out of 1 in the Crystal Structure of Mevalonate Kinase From Methicillin- Resistant Staphylococcus Aureus MRSA252


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 Mevalonate Kinase From Methicillin- Resistant Staphylococcus Aureus MRSA252 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1308

b:47.5
occ:1.00
O A:HOH2020 3.1 37.1 1.0
OG1 A:THR266 3.2 47.6 1.0
NH1 A:ARG270 3.2 47.3 1.0
N A:GLY272 3.4 49.2 1.0
CA A:GLY272 3.6 49.5 1.0
CD A:ARG270 3.7 48.3 1.0
CA A:GLY267 3.9 47.6 1.0
CB A:ARG270 3.9 48.9 1.0
CG A:ARG270 3.9 48.4 1.0
CD2 A:HIS19 4.0 47.2 1.0
C A:THR266 4.0 47.6 1.0
N A:GLY267 4.0 47.4 1.0
O A:THR266 4.0 48.7 1.0
CB A:THR266 4.1 47.5 1.0
O A:ARG97 4.1 47.7 1.0
CB A:HIS19 4.2 48.9 1.0
CZ A:ARG270 4.2 48.4 1.0
N A:GLY271 4.3 49.5 1.0
CG A:HIS19 4.4 48.2 1.0
NE A:ARG270 4.4 49.1 1.0
C A:ARG97 4.5 47.7 1.0
CA A:GLY98 4.5 46.5 1.0
C A:GLY271 4.6 50.1 1.0
CA A:THR266 4.7 47.5 1.0
N A:GLY98 4.7 46.9 1.0
O A:HOH2058 4.7 43.9 1.0
C A:ARG270 4.8 50.1 1.0
C A:GLY272 4.8 49.6 1.0
CA A:HIS19 4.8 48.4 1.0
N A:SER273 4.8 49.1 1.0
CA A:ARG270 4.9 49.8 1.0
CA A:GLY271 5.0 49.8 1.0

Reference:

M.Oke, L.G.Carter, K.A.Johnson, H.Liu, S.A.Mcmahon, X.Yan, M.Kerou, N.D.Weikart, N.Kadi, M.A.Sheikh, S.Schmelz, M.Dorward, M.Zawadzki, C.Cozens, H.Falconer, H.Powers, I.M.Overton, C.A.J.Van Niekerk, X.Peng, P.Patel, R.A.Garrett, D.Prangishvili, C.H.Botting, P.J.Coote, D.T.F.Dryden, G.J.Barton, U.Schwarz-Linek, G.L.Challis, G.L.Taylor, M.F.White, J.H.Naismith. The Scottish Structural Proteomics Facility: Targets, Methods and Outputs. J.Struct.Funct.Genomics V. 11 167 2010.
ISSN: ISSN 1345-711X
PubMed: 20419351
DOI: 10.1007/S10969-010-9090-Y
Page generated: Fri Jul 11 01:48:22 2025

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