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Chlorine in PDB 4kkv: Crystal Structure of Candida Glabrata Fmn Adenylyltransferase D181A Mutant

Enzymatic activity of Crystal Structure of Candida Glabrata Fmn Adenylyltransferase D181A Mutant

All present enzymatic activity of Crystal Structure of Candida Glabrata Fmn Adenylyltransferase D181A Mutant:
2.7.7.2;

Protein crystallography data

The structure of Crystal Structure of Candida Glabrata Fmn Adenylyltransferase D181A Mutant, PDB code: 4kkv was solved by C.Huerta, H.Zhang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.40 / 1.74
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 80.257, 80.257, 78.169, 90.00, 90.00, 120.00
R / Rfree (%) 17.2 / 20.1

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Candida Glabrata Fmn Adenylyltransferase D181A Mutant (pdb code 4kkv). 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 Crystal Structure of Candida Glabrata Fmn Adenylyltransferase D181A Mutant, PDB code: 4kkv:

Chlorine binding site 1 out of 1 in 4kkv

Go back to Chlorine Binding Sites List in 4kkv
Chlorine binding site 1 out of 1 in the Crystal Structure of Candida Glabrata Fmn Adenylyltransferase D181A Mutant


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Candida Glabrata Fmn Adenylyltransferase D181A Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl402

b:22.6
occ:1.00
OH A:TYR216 2.9 15.5 1.0
O A:HOH583 3.3 25.5 1.0
N A:LEU223 3.3 18.5 1.0
NZ A:LYS65 3.3 16.9 1.0
O A:HOH785 3.4 41.7 1.0
O A:HOH598 3.7 29.2 1.0
CA A:SER222 3.7 16.6 1.0
CZ A:TYR216 3.8 14.2 1.0
CE1 A:TYR216 3.9 13.9 1.0
C A:SER222 4.0 17.9 1.0
CG A:LEU223 4.0 19.6 1.0
CB A:LEU223 4.1 19.3 1.0
O A:THR221 4.2 15.0 1.0
CG A:LYS65 4.2 16.6 1.0
CA A:LEU223 4.2 18.9 1.0
CD A:LYS65 4.4 17.1 1.0
CE A:LYS65 4.4 16.9 1.0
OG A:SER222 4.4 17.6 1.0
N A:LYS65 4.4 15.7 1.0
CA A:GLY64 4.6 15.6 1.0
CB A:SER222 4.6 17.1 1.0
N A:SER222 4.6 15.6 1.0
CD1 A:LEU223 4.6 20.0 1.0
C A:THR221 4.8 14.9 1.0
O A:LEU223 4.8 21.3 1.0
C A:LEU223 4.9 19.9 1.0

Reference:

C.Huerta, N.V.Grishin, H.Zhang. The "Super Mutant" of Yeast Fmn Adenylyltransferase Enhances the Enzyme Turnover Rate By Attenuating Product Inhibition. Biochemistry V. 52 3615 2013.
ISSN: ISSN 0006-2960
PubMed: 23663086
DOI: 10.1021/BI400454W
Page generated: Sun Jul 21 18:11:59 2024

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