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Chlorine in PDB 4h9f: Radiation Damage Study of Lysozyme - 0.91 Mgy

Enzymatic activity of Radiation Damage Study of Lysozyme - 0.91 Mgy

All present enzymatic activity of Radiation Damage Study of Lysozyme - 0.91 Mgy:
3.2.1.17;

Protein crystallography data

The structure of Radiation Damage Study of Lysozyme - 0.91 Mgy, PDB code: 4h9f was solved by K.A.Sutton, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 26.92 / 1.20
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 78.771, 78.771, 36.869, 90.00, 90.00, 90.00
R / Rfree (%) 19.3 / 20.4

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Radiation Damage Study of Lysozyme - 0.91 Mgy (pdb code 4h9f). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Radiation Damage Study of Lysozyme - 0.91 Mgy, PDB code: 4h9f:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in 4h9f

Go back to Chlorine Binding Sites List in 4h9f
Chlorine binding site 1 out of 3 in the Radiation Damage Study of Lysozyme - 0.91 Mgy


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Radiation Damage Study of Lysozyme - 0.91 Mgy within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl201

b:13.1
occ:1.00
ND2 A:ASN113 3.3 11.2 1.0
CB A:ASN113 3.6 10.0 1.0
CA A:ALA110 3.8 13.5 1.0
CG A:ASN113 4.0 11.3 1.0
CB A:ALA110 4.2 13.8 1.0
N A:ALA110 4.2 11.2 1.0
O A:VAL109 4.3 13.5 1.0
CD A:ARG114 4.3 11.1 1.0
CG1 A:VAL109 4.4 21.3 1.0
C A:VAL109 4.5 14.0 1.0
CG A:ARG114 4.5 10.7 1.0
C A:ALA110 4.9 11.3 1.0
CA A:ASN113 5.0 10.5 1.0
O A:ALA110 5.0 11.4 1.0

Chlorine binding site 2 out of 3 in 4h9f

Go back to Chlorine Binding Sites List in 4h9f
Chlorine binding site 2 out of 3 in the Radiation Damage Study of Lysozyme - 0.91 Mgy


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Radiation Damage Study of Lysozyme - 0.91 Mgy within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl202

b:13.4
occ:1.00
O A:HOH306 3.1 10.6 1.0
N A:THR69 3.2 10.1 1.0
O A:HOH349 3.2 19.8 1.0
O A:THR69 3.3 11.5 1.0
N A:ARG68 3.4 10.8 0.5
N A:ARG68 3.5 10.9 0.5
C A:GLY67 3.5 10.8 1.0
O A:HOH387 3.5 25.3 1.0
CA A:GLY67 3.6 11.1 1.0
N A:GLY67 3.7 10.0 1.0
OG A:SER72 3.7 13.9 1.0
C A:THR69 3.7 10.5 1.0
OD1 A:ASN65 3.8 11.1 1.0
CA A:THR69 3.8 10.9 1.0
O A:HOH315 4.1 12.9 1.0
O A:GLY67 4.2 13.2 1.0
C A:ARG68 4.2 12.4 0.5
CB A:THR69 4.2 9.8 1.0
C A:ARG68 4.2 12.4 0.5
OD1 A:ASP66 4.2 8.9 1.0
CA A:ARG68 4.2 11.9 0.5
CA A:ARG68 4.3 11.6 0.5
N A:PRO70 4.5 11.5 1.0
O A:HOH301 4.7 6.9 1.0
C A:ASP66 4.7 9.1 1.0
OG1 A:THR69 4.8 10.1 1.0
O A:HOH343 4.8 17.1 0.5
N A:ASP66 4.9 8.4 1.0
CB A:SER72 4.9 13.2 1.0
CG A:ASN65 5.0 11.7 1.0

Chlorine binding site 3 out of 3 in 4h9f

Go back to Chlorine Binding Sites List in 4h9f
Chlorine binding site 3 out of 3 in the Radiation Damage Study of Lysozyme - 0.91 Mgy


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Radiation Damage Study of Lysozyme - 0.91 Mgy within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl203

b:16.3
occ:1.00
OG A:SER24 3.0 14.2 1.0
N A:GLY26 3.1 10.2 1.0
CB A:SER24 3.5 13.8 1.0
CA A:GLY26 3.5 11.1 1.0
CA A:GLN121 3.6 14.6 1.0
CD1 A:ILE124 3.8 21.2 1.0
CB A:GLN121 3.9 17.6 1.0
N A:GLN121 4.0 14.1 1.0
CG A:GLN121 4.1 27.8 1.0
CG1 A:ILE124 4.2 18.9 1.0
N A:LEU25 4.2 10.4 1.0
C A:VAL120 4.3 12.8 1.0
O A:VAL120 4.3 11.9 1.0
CG2 A:VAL120 4.3 14.6 1.0
C A:LEU25 4.3 10.4 1.0
C A:SER24 4.4 10.7 1.0
C A:GLY26 4.5 8.7 1.0
CA A:SER24 4.6 11.1 1.0
N A:ASN27 4.6 9.4 1.0
CA A:LEU25 4.7 11.2 1.0
O A:HOH388 4.8 22.7 1.0
C A:GLN121 4.8 13.0 1.0
O A:SER24 4.9 11.4 1.0

Reference:

K.A.Sutton, P.J.Black, K.R.Mercer, E.F.Garman, R.L.Owen, E.H.Snell, W.A.Bernhard. Insights Into the Mechanism of X-Ray-Induced Disulfide-Bond Cleavage in Lysozyme Crystals Based on Epr, Optical Absorption and X-Ray Diffraction Studies. Acta Crystallogr.,Sect.D V. 69 2381 2013.
ISSN: ISSN 0907-4449
PubMed: 24311579
DOI: 10.1107/S0907444913022117
Page generated: Sat Dec 12 10:42:04 2020

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