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Chlorine in PDB 5n2p: Sulfolobus Solfataricus Tryptophan Synthase A

Enzymatic activity of Sulfolobus Solfataricus Tryptophan Synthase A

All present enzymatic activity of Sulfolobus Solfataricus Tryptophan Synthase A:
4.2.1.20;

Protein crystallography data

The structure of Sulfolobus Solfataricus Tryptophan Synthase A, PDB code: 5n2p was solved by J.Fleming, O.Mayans, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.27 / 2.06
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 76.540, 76.540, 122.000, 90.00, 90.00, 90.00
R / Rfree (%) 22.6 / 24.8

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Sulfolobus Solfataricus Tryptophan Synthase A (pdb code 5n2p). 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 Sulfolobus Solfataricus Tryptophan Synthase A, PDB code: 5n2p:

Chlorine binding site 1 out of 1 in 5n2p

Go back to Chlorine Binding Sites List in 5n2p
Chlorine binding site 1 out of 1 in the Sulfolobus Solfataricus Tryptophan Synthase A


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Sulfolobus Solfataricus Tryptophan Synthase A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl303

b:42.7
occ:1.00
N A:ARG160 3.0 34.9 1.0
O A:HOH464 3.1 45.8 1.0
NH1 A:ARG160 3.2 31.0 1.0
N A:ILE167 3.5 40.7 1.0
CA A:ARG160 3.6 42.5 1.0
CG1 A:ILE167 3.8 44.5 1.0
CD A:PRO161 3.9 46.3 1.0
CB A:ILE167 4.0 32.2 1.0
C A:VAL159 4.1 37.7 1.0
CD A:ARG160 4.1 33.7 1.0
CB A:VAL159 4.1 37.4 1.0
CA A:PRO166 4.1 49.5 1.0
CA A:VAL159 4.2 38.8 1.0
CD1 A:ILE167 4.2 38.0 1.0
CD1 A:LEU174 4.2 39.0 1.0
CB A:PRO166 4.2 52.6 1.0
CA A:ILE167 4.3 39.9 1.0
C A:PRO166 4.3 54.4 1.0
CZ A:ARG160 4.4 40.4 1.0
CG A:ARG160 4.4 39.9 1.0
O A:ILE167 4.6 40.6 1.0
CB A:ARG160 4.6 31.4 1.0
NE A:ARG160 4.7 39.0 1.0
N A:PRO161 4.7 48.6 1.0
C A:ARG160 4.7 44.9 1.0
C A:ILE167 5.0 42.0 1.0
CG1 A:VAL159 5.0 31.4 1.0
O A:HOH434 5.0 49.1 1.0

Reference:

J.R.Fleming, M.Schupfner, F.Busch, A.Basle, A.Ehrmann, R.Sterner, O.Mayans. Evolutionary Morphing of Tryptophan Synthase: Functional Mechanisms For the Enzymatic Channeling of Indole. J.Mol.Biol. V. 430 5066 2018.
ISSN: ESSN 1089-8638
PubMed: 30367843
DOI: 10.1016/J.JMB.2018.10.013
Page generated: Sat Dec 12 12:08:20 2020

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