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Chlorine in PDB 3s1u: Transaldolase From Thermoplasma Acidophilum in Complex with D- Erythrose 4-Phosphate

Enzymatic activity of Transaldolase From Thermoplasma Acidophilum in Complex with D- Erythrose 4-Phosphate

All present enzymatic activity of Transaldolase From Thermoplasma Acidophilum in Complex with D- Erythrose 4-Phosphate:
2.2.1.2;

Protein crystallography data

The structure of Transaldolase From Thermoplasma Acidophilum in Complex with D- Erythrose 4-Phosphate, PDB code: 3s1u was solved by A.Lehwess-Litzmann, P.Neumann, C.Parthier, K.Tittmann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.85 / 1.90
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 148.200, 171.400, 99.100, 90.00, 90.00, 90.00
R / Rfree (%) 17.5 / 19.9

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Transaldolase From Thermoplasma Acidophilum in Complex with D- Erythrose 4-Phosphate (pdb code 3s1u). 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 Transaldolase From Thermoplasma Acidophilum in Complex with D- Erythrose 4-Phosphate, PDB code: 3s1u:

Chlorine binding site 1 out of 1 in 3s1u

Go back to Chlorine Binding Sites List in 3s1u
Chlorine binding site 1 out of 1 in the Transaldolase From Thermoplasma Acidophilum in Complex with D- Erythrose 4-Phosphate


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Transaldolase From Thermoplasma Acidophilum in Complex with D- Erythrose 4-Phosphate within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl224

b:28.0
occ:0.50
ND2 C:ASN170 3.1 19.7 1.0
O C:HOH232 3.4 29.8 1.0
O C:HOH244 3.6 20.4 1.0
CB C:ARG169 3.8 21.8 1.0
CB C:ASN170 4.0 16.3 1.0
CG C:ASN170 4.0 21.4 1.0
O C:ARG169 4.3 20.6 1.0
C C:ARG169 4.5 21.3 1.0
CG C:ARG169 4.8 20.8 1.0
CA C:ARG169 4.8 19.5 1.0
N C:ASN170 4.9 16.8 1.0
O C:HOH269 4.9 36.4 1.0

Reference:

A.Lehwess-Litzmann, P.Neumann, C.Parthier, S.Ludtke, R.Golbik, R.Ficner, K.Tittmann. Twisted Schiff Base Intermediates and Substrate Locale Revise Transaldolase Mechanism. Nat.Chem.Biol. V. 7 678 2011.
ISSN: ISSN 1552-4450
PubMed: 21857661
DOI: 10.1038/NCHEMBIO.633
Page generated: Fri Jul 11 10:04:45 2025

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