Chlorine in PDB 7wkr: Room Temperature Structure of Lysozyme Solved By Serial Synchrotron Crystallography

Enzymatic activity of Room Temperature Structure of Lysozyme Solved By Serial Synchrotron Crystallography

All present enzymatic activity of Room Temperature Structure of Lysozyme Solved By Serial Synchrotron Crystallography:
3.2.1.17;

Protein crystallography data

The structure of Room Temperature Structure of Lysozyme Solved By Serial Synchrotron Crystallography, PDB code: 7wkr was solved by K.H.Nam, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 55.53 / 1.60
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 78.53, 78.53, 38, 90, 90, 90
R / Rfree (%) 17.3 / 19.8

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Room Temperature Structure of Lysozyme Solved By Serial Synchrotron Crystallography (pdb code 7wkr). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Room Temperature Structure of Lysozyme Solved By Serial Synchrotron Crystallography, PDB code: 7wkr:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 7wkr

Go back to Chlorine Binding Sites List in 7wkr
Chlorine binding site 1 out of 2 in the Room Temperature Structure of Lysozyme Solved By Serial Synchrotron Crystallography


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Room Temperature Structure of Lysozyme Solved By Serial Synchrotron Crystallography within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl201

b:39.1
occ:1.00
HH A:TYR41 2.2 36.8 1.0
OH A:TYR41 2.9 30.6 1.0
HE2 A:TYR41 3.1 34.1 1.0
HA3 A:GLY122 3.3 37.3 1.0
CZ A:TYR41 3.6 25.7 1.0
CE2 A:TYR41 3.6 28.4 1.0
HA2 A:GLY122 3.9 37.3 1.0
CA A:GLY122 4.0 31.0 1.0
HH21 A:ARG39 4.5 82.0 1.0
N A:GLY122 4.6 31.0 1.0
O A:ARG39 4.6 35.3 1.0
O A:HOH312 4.7 43.6 1.0
H A:MET123 4.7 32.8 1.0
H A:GLY122 4.8 37.3 1.0
CE1 A:TYR41 4.9 27.5 1.0
CD2 A:TYR41 4.9 28.2 1.0
HE A:ARG39 4.9 87.0 1.0
HB3 A:ARG39 5.0 45.5 1.0

Chlorine binding site 2 out of 2 in 7wkr

Go back to Chlorine Binding Sites List in 7wkr
Chlorine binding site 2 out of 2 in the Room Temperature Structure of Lysozyme Solved By Serial Synchrotron Crystallography


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Room Temperature Structure of Lysozyme Solved By Serial Synchrotron Crystallography within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl202

b:46.9
occ:1.00
H A:GLY44 2.2 36.2 1.0
HG A:SER42 2.6 41.2 1.0
HA A:GLN139 2.8 44.2 1.0
HB2 A:SER42 2.8 42.7 1.0
HA3 A:GLY44 2.9 35.6 1.0
OG A:SER42 2.9 34.3 1.0
N A:GLY44 3.0 30.2 1.0
CB A:SER42 3.4 35.5 1.0
HD11 A:ILE142 3.4 67.2 1.0
CA A:GLY44 3.4 29.6 1.0
HB2 A:GLN139 3.5 56.5 1.0
HG23 A:VAL138 3.5 42.1 1.0
HG12 A:ILE142 3.5 43.9 1.0
CA A:GLN139 3.6 36.8 1.0
HG2 A:GLN139 3.7 80.3 1.0
HD13 A:ILE142 3.9 67.2 1.0
CB A:GLN139 3.9 47.0 1.0
CD1 A:ILE142 4.0 55.9 1.0
H A:LEU43 4.0 38.9 1.0
N A:LEU43 4.0 32.4 1.0
HA2 A:GLY44 4.0 35.6 1.0
HB3 A:SER42 4.0 42.7 1.0
N A:GLN139 4.0 36.7 1.0
C A:SER42 4.1 33.8 1.0
C A:LEU43 4.1 29.8 1.0
HB3 A:LEU43 4.2 38.0 1.0
H A:ASN45 4.2 32.5 1.0
CG1 A:ILE142 4.2 36.6 1.0
CG A:GLN139 4.3 66.9 1.0
O A:VAL138 4.3 38.1 1.0
C A:VAL138 4.4 35.7 1.0
H A:GLN139 4.4 44.1 1.0
CA A:SER42 4.4 32.2 1.0
CG2 A:VAL138 4.4 35.1 1.0
CA A:LEU43 4.5 28.6 1.0
C A:GLY44 4.5 29.7 1.0
O A:SER42 4.5 30.7 1.0
HG13 A:ILE142 4.6 43.9 1.0
HG21 A:VAL138 4.6 42.1 1.0
N A:ASN45 4.7 27.0 1.0
HG3 A:GLN139 4.8 80.3 1.0
CB A:LEU43 4.8 31.6 1.0
HB3 A:GLN139 4.8 56.5 1.0
C A:GLN139 4.8 34.8 1.0
HD12 A:ILE142 4.9 67.2 1.0
HB A:VAL138 4.9 40.0 1.0
HG21 A:ILE142 4.9 44.5 1.0
HA A:SER42 4.9 38.7 1.0
HD22 A:ASN45 4.9 41.8 1.0
HG22 A:VAL138 5.0 42.1 1.0

Reference:

K.Lee, J.Kim, S.Baek, J.Park, S.Park, J.L.Lee, W.K.Chung, Y.Cho, K.H.Nam. Combination of An Inject-and-Transfer System For Serial Femtosecond Crystallography. J.Appl.Crystallogr. V. 55 813 2022.
ISSN: ISSN 0021-8898
PubMed: 35979068
DOI: 10.1107/S1600576722005556
Page generated: Tue Jul 30 05:38:41 2024

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