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Calcium in PDB 4kxv: Human Transketolase in Covalent Complex with Donor Ketose D-Xylulose- 5-Phosphate, Crystal 1

Enzymatic activity of Human Transketolase in Covalent Complex with Donor Ketose D-Xylulose- 5-Phosphate, Crystal 1

All present enzymatic activity of Human Transketolase in Covalent Complex with Donor Ketose D-Xylulose- 5-Phosphate, Crystal 1:
2.2.1.1;

Protein crystallography data

The structure of Human Transketolase in Covalent Complex with Donor Ketose D-Xylulose- 5-Phosphate, Crystal 1, PDB code: 4kxv was solved by P.Neumann, S.Luedtke, R.Ficner, K.Tittmann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 0.97
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 113.670, 85.980, 73.000, 90.00, 125.30, 90.00
R / Rfree (%) 9.4 / 11.4

Calcium Binding Sites:

The binding sites of Calcium atom in the Human Transketolase in Covalent Complex with Donor Ketose D-Xylulose- 5-Phosphate, Crystal 1 (pdb code 4kxv). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Human Transketolase in Covalent Complex with Donor Ketose D-Xylulose- 5-Phosphate, Crystal 1, PDB code: 4kxv:

Calcium binding site 1 out of 1 in 4kxv

Go back to Calcium Binding Sites List in 4kxv
Calcium binding site 1 out of 1 in the Human Transketolase in Covalent Complex with Donor Ketose D-Xylulose- 5-Phosphate, Crystal 1


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Human Transketolase in Covalent Complex with Donor Ketose D-Xylulose- 5-Phosphate, Crystal 1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca1001

b:3.2
occ:0.64
 OD1 A:ASP155 2.0 4.1 1.0
O13 A:TDP1011 2.0 3.5 1.0
O A:LEU187 2.1 4.0 1.0
O21 A:TDP1011 2.1 3.6 1.0
OD1 A:ASN185 2.1 3.5 1.0
O A:HOH7001 2.2 3.7 1.0
CG A:ASN185 3.1 3.6 1.0
P2 A:TDP1011 3.2 3.5 1.0
CG A:ASP155 3.2 3.8 1.0
C A:LEU187 3.3 3.4 1.0
P1 A:TDP1011 3.3 3.4 1.0
ND2 A:ASN185 3.4 4.2 1.0
O11 A:TDP1011 3.4 3.7 1.0
O22 A:TDP1011 3.7 4.5 1.0
OD2 A:ASP155 3.9 5.2 1.0
N A:ASP155 4.0 3.6 1.0
N A:LEU187 4.0 3.9 1.0
O5G A:TDP1011 4.1 4.0 1.0
N A:GLY156 4.1 3.6 1.0
N A:GLY188 4.2 3.9 1.0
CA A:LEU187 4.2 3.9 1.0
NZ A:LYS244 4.3 4.3 1.0
CB A:ASP155 4.3 4.1 1.0
O A:ASP183 4.3 4.2 1.0
CA A:GLY188 4.3 4.0 1.0
O12 A:TDP1011 4.4 3.7 1.0
CB A:ASN185 4.4 3.9 1.0
O23 A:TDP1011 4.5 4.5 1.0
CA A:ASP155 4.5 3.3 1.0
N A:ASN185 4.5 3.7 1.0
C A:ASN185 4.7 3.7 1.0
CA A:ASN185 4.7 3.6 1.0
N A:ARG186 4.7 3.9 1.0
CD A:LYS244 4.7 3.9 1.0
C A:ASP155 4.8 3.5 1.0
CB A:LEU187 4.9 4.6 1.0
C A:ARG186 4.9 3.9 1.0
CE A:LYS244 5.0 4.0 1.0
C A:GLY154 5.0 4.1 1.0

Reference:

S.Ludtke, P.Neumann, K.M.Erixon, F.Leeper, R.Kluger, R.Ficner, K.Tittmann. Sub-Angstrom-Resolution Crystallography Reveals Physical Distortions That Enhance Reactivity of A Covalent Enzymatic Intermediate. Nat Chem V. 5 762 2013.
PubMed: 23965678
DOI: 10.1038/NCHEM.1728
Page generated: Sat Dec 12 04:55:53 2020

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