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Chlorine in PDB 1cx7: T4 Lysozyme Methionine Core Mutant

Enzymatic activity of T4 Lysozyme Methionine Core Mutant

All present enzymatic activity of T4 Lysozyme Methionine Core Mutant:
3.2.1.17;

Protein crystallography data

The structure of T4 Lysozyme Methionine Core Mutant, PDB code: 1cx7 was solved by N.C.Gassner, W.A.Baase, J.Lindstrom, J.Lu, B.W.Matthews, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.94
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 61.310, 61.310, 96.490, 90.00, 90.00, 120.00
R / Rfree (%) n/a / n/a

Chlorine Binding Sites:

The binding sites of Chlorine atom in the T4 Lysozyme Methionine Core Mutant (pdb code 1cx7). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the T4 Lysozyme Methionine Core Mutant, PDB code: 1cx7:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 1cx7

Go back to Chlorine Binding Sites List in 1cx7
Chlorine binding site 1 out of 2 in the T4 Lysozyme Methionine Core Mutant


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of T4 Lysozyme Methionine Core Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl178

b:32.2
occ:0.50
O A:HOH215 3.0 19.4 1.0
O A:HOH182 3.1 22.8 1.0
O A:HOH200 3.4 48.4 1.0
CE1 A:HIS31 3.8 12.9 1.0
CB A:ALA49 3.9 16.8 1.0
NE2 A:HIS31 3.9 16.4 1.0
NE2 A:GLN69 4.2 12.6 1.0
CA A:ALA49 4.6 18.2 1.0
CD2 A:LEU66 4.6 16.3 1.0
O A:HOH282 4.7 42.7 1.0
ND1 A:HIS31 5.0 12.8 1.0

Chlorine binding site 2 out of 2 in 1cx7

Go back to Chlorine Binding Sites List in 1cx7
Chlorine binding site 2 out of 2 in the T4 Lysozyme Methionine Core Mutant


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of T4 Lysozyme Methionine Core Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl173

b:29.6
occ:1.00
O A:HOH209 3.0 36.9 1.0
N A:ARG145 3.5 15.0 1.0
CA A:THR142 3.6 4.4 1.0
C A:THR142 3.6 11.1 1.0
CB A:THR142 3.6 15.4 1.0
N A:ASN144 3.6 10.4 1.0
CB A:ASN144 3.9 15.8 1.0
N A:PRO143 4.0 16.8 1.0
O A:THR142 4.0 12.2 1.0
CB A:ARG145 4.1 13.3 1.0
CA A:ASN144 4.1 8.8 1.0
CG2 A:THR142 4.3 14.2 1.0
C A:ASN144 4.3 18.3 1.0
CD A:PRO143 4.3 10.9 1.0
O A:HOH336 4.3 58.1 1.0
O A:HOH230 4.4 55.9 1.0
CA A:ARG145 4.4 10.2 1.0
C A:PRO143 4.5 13.9 1.0
CA A:PRO143 4.8 12.4 1.0
OG1 A:THR142 4.8 18.8 1.0
CG A:ASN144 4.8 16.3 1.0
ND2 A:ASN144 4.9 23.0 1.0
N A:THR142 5.0 10.3 1.0

Reference:

N.C.Gassner, B.W.Matthews. Use of Differentially Substituted Selenomethionine Proteins in X-Ray Structure Determination. Acta Crystallogr.,Sect.D V. 55 1967 1999.
ISSN: ISSN 0907-4449
PubMed: 10666571
DOI: 10.1021/BI9915519
Page generated: Fri Jul 19 21:30:19 2024

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