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Chlorine in PDB 1xjn: Structural Mechanism of Allosteric Substrate Specificity in A Ribonucleotide Reductase: Datp-Cdp Complex

Enzymatic activity of Structural Mechanism of Allosteric Substrate Specificity in A Ribonucleotide Reductase: Datp-Cdp Complex

All present enzymatic activity of Structural Mechanism of Allosteric Substrate Specificity in A Ribonucleotide Reductase: Datp-Cdp Complex:
1.17.4.1;

Protein crystallography data

The structure of Structural Mechanism of Allosteric Substrate Specificity in A Ribonucleotide Reductase: Datp-Cdp Complex, PDB code: 1xjn was solved by K.-M.Larsson, A.Jordan, R.Eliasson, P.Reichard, D.T.Logan, P.Nordlund, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.54 / 2.25
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 105.970, 123.830, 117.410, 90.00, 104.02, 90.00
R / Rfree (%) 19 / 25.4

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structural Mechanism of Allosteric Substrate Specificity in A Ribonucleotide Reductase: Datp-Cdp Complex (pdb code 1xjn). 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 Structural Mechanism of Allosteric Substrate Specificity in A Ribonucleotide Reductase: Datp-Cdp Complex, PDB code: 1xjn:

Chlorine binding site 1 out of 1 in 1xjn

Go back to Chlorine Binding Sites List in 1xjn
Chlorine binding site 1 out of 1 in the Structural Mechanism of Allosteric Substrate Specificity in A Ribonucleotide Reductase: Datp-Cdp Complex


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structural Mechanism of Allosteric Substrate Specificity in A Ribonucleotide Reductase: Datp-Cdp Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl1009

b:58.0
occ:1.00
 NH1 B:ARG207 2.4 70.8 1.0
NH2 B:ARG207 2.8 70.8 1.0
CZ B:ARG207 3.0 71.4 1.0
O B:HOH1027 3.2 22.4 1.0
O B:HOH1119 3.2 23.3 1.0
O1B B:CDP1001 3.6 29.3 1.0
CB B:SER91 3.7 18.5 1.0
N1 B:CDP1001 3.8 39.0 1.0
C6 B:CDP1001 3.8 38.9 1.0
C2 B:CDP1001 4.0 38.9 1.0
C5 B:CDP1001 4.0 41.0 1.0
CD B:PRO92 4.0 14.6 1.0
O B:HOH1160 4.0 27.5 1.0
N3 B:CDP1001 4.2 41.2 1.0
C4 B:CDP1001 4.2 41.3 1.0
OG B:SER91 4.2 21.6 1.0
NE B:ARG207 4.3 72.4 1.0
C1' B:CDP1001 4.4 38.5 1.0
O4' B:CDP1001 4.4 34.2 1.0
CG B:PRO92 4.4 15.8 1.0
PB B:CDP1001 4.5 24.7 1.0
OE1 B:GLN203 4.5 51.2 1.0
O3A B:CDP1001 4.5 27.7 1.0
O2 B:CDP1001 4.5 39.6 1.0
CE2 B:PHE95 4.5 22.2 1.0
O2B B:CDP1001 4.7 26.1 1.0
N B:PRO92 4.7 16.2 1.0
CA B:SER91 4.7 17.9 1.0
N B:SER91 4.9 18.5 1.0
N4 B:CDP1001 5.0 40.2 1.0

Reference:

K.-M.Larsson, A.Jordan, R.Eliasson, P.Reichard, D.T.Logan, P.Nordlund. Structural Mechanism of Allosteric Substrate Specificity Regulation in A Ribonucleotide Reductase Nat.Struct.Mol.Biol. V. 11 1142 2004.
ISSN: ISSN 1545-9993
PubMed: 15475969
DOI: 10.1038/NSMB838
Page generated: Sat Dec 12 08:54:39 2020

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