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Chlorine in PDB 1qug: E108V Mutant of T4 Lysozyme

Enzymatic activity of E108V Mutant of T4 Lysozyme

All present enzymatic activity of E108V Mutant of T4 Lysozyme:
3.2.1.17;

Protein crystallography data

The structure of E108V Mutant of T4 Lysozyme, PDB code: 1qug was solved by J.Wray, W.A.Baase, J.D.Lindstrom, A.R.Poteete, B.W.Matthews, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.90
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 60.920, 60.920, 97.250, 90.00, 90.00, 120.00
R / Rfree (%) n/a / n/a

Chlorine Binding Sites:

The binding sites of Chlorine atom in the E108V Mutant of T4 Lysozyme (pdb code 1qug). 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 E108V Mutant of T4 Lysozyme, PDB code: 1qug:

Chlorine binding site 1 out of 1 in 1qug

Go back to Chlorine Binding Sites List in 1qug
Chlorine binding site 1 out of 1 in the E108V Mutant of T4 Lysozyme


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of E108V Mutant of T4 Lysozyme within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl500

b:35.0
occ:1.00
O A:HOH209 2.9 35.6 1.0
N A:ARG145 3.2 11.3 1.0
N A:ASN144 3.2 2.8 1.0
C A:THR142 3.5 21.7 1.0
CB A:THR142 3.6 18.6 1.0
CA A:THR142 3.6 2.7 1.0
O A:THR142 3.7 13.0 1.0
CA A:ASN144 3.8 10.4 1.0
CB A:ASN144 3.8 18.1 1.0
N A:PRO143 3.8 14.8 1.0
CB A:ARG145 3.8 8.9 1.0
C A:ASN144 4.0 20.8 1.0
CA A:ARG145 4.1 10.2 1.0
C A:PRO143 4.1 15.1 1.0
CG2 A:THR142 4.2 6.2 1.0
CD A:PRO143 4.3 14.7 1.0
CA A:PRO143 4.5 19.6 1.0
CG A:ASN144 4.6 26.8 1.0
O A:HOH230 4.6 29.2 1.0
ND2 A:ASN144 4.8 24.2 1.0
OG1 A:THR142 4.8 12.7 1.0

Reference:

J.W.Wray, W.A.Baase, J.D.Lindstrom, L.H.Weaver, A.R.Poteete, B.W.Matthews. Structural Analysis of A Non-Contiguous Second-Site Revertant in T4 Lysozyme Shows That Increasing the Rigidity of A Protein Can Enhance Its Stability. J.Mol.Biol. V. 292 1111 1999.
ISSN: ISSN 0022-2836
PubMed: 10512706
DOI: 10.1006/JMBI.1999.3102
Page generated: Sat Jul 20 01:43:36 2024

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