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Chlorine in PDB 4irb: Crystal Structure of Vaccinia Virus Uracil Dna Glycosylase Mutant DEL171-172D4

Enzymatic activity of Crystal Structure of Vaccinia Virus Uracil Dna Glycosylase Mutant DEL171-172D4

All present enzymatic activity of Crystal Structure of Vaccinia Virus Uracil Dna Glycosylase Mutant DEL171-172D4:
3.2.2.27;

Protein crystallography data

The structure of Crystal Structure of Vaccinia Virus Uracil Dna Glycosylase Mutant DEL171-172D4, PDB code: 4irb was solved by N.Schormann, N.Zhukovskaya, D.Sartmatova, M.Nuth, R.P.Ricciardi, D.Chattopadhyay, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.64 / 2.30
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 101.900, 130.510, 86.310, 90.00, 90.00, 90.00
R / Rfree (%) 21.1 / 25.8

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Vaccinia Virus Uracil Dna Glycosylase Mutant DEL171-172D4 (pdb code 4irb). 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 Vaccinia Virus Uracil Dna Glycosylase Mutant DEL171-172D4, PDB code: 4irb:

Chlorine binding site 1 out of 1 in 4irb

Go back to Chlorine Binding Sites List in 4irb
Chlorine binding site 1 out of 1 in the Crystal Structure of Vaccinia Virus Uracil Dna Glycosylase Mutant DEL171-172D4


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 Vaccinia Virus Uracil Dna Glycosylase Mutant DEL171-172D4 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl302

b:41.6
occ:1.00
O B:HOH430 2.9 50.8 1.0
O B:HOH412 3.2 42.4 1.0
N B:TYR70 3.3 34.4 1.0
N B:PHE79 3.3 27.6 1.0
CD2 B:TYR70 3.3 31.0 1.0
ND2 B:ASN120 3.3 44.5 1.0
CA B:PRO69 3.5 33.9 1.0
O B:HOH409 3.5 26.5 1.0
CE2 B:TYR70 3.8 34.2 1.0
CB B:PRO69 3.8 31.2 1.0
CA B:PRO78 3.9 29.6 1.0
C B:PRO69 3.9 29.9 1.0
CG B:TYR70 4.1 35.0 1.0
C B:PRO78 4.1 28.2 1.0
CA B:PHE79 4.2 27.9 1.0
O B:VAL77 4.2 40.2 1.0
CG B:ASN120 4.3 45.5 1.0
CA B:TYR70 4.4 36.9 1.0
CB B:TYR70 4.5 36.7 1.0
OD1 B:ASN120 4.5 48.6 1.0
O B:HOH429 4.5 41.5 1.0
O B:HOH428 4.6 39.6 1.0
N B:PRO78 4.6 29.1 1.0
N B:PRO69 4.7 36.8 1.0
C B:VAL77 4.7 38.1 1.0
CZ B:TYR70 4.7 37.8 1.0
CG B:PRO69 4.8 32.5 1.0
N B:GLU80 4.9 29.8 1.0
O B:ASP68 4.9 28.0 1.0
C B:PHE79 4.9 31.8 1.0
CA B:GLY74 4.9 40.9 1.0
CB B:PRO78 4.9 29.3 1.0
CD1 B:TYR70 5.0 31.9 1.0

Reference:

N.Schormann, N.Zhukovskaya, D.Sartmatova, M.Nuth, R.P.Ricciardi, D.Chattopadhyay. Mutations at the Dimer Interface Affect Both Function and Structure of the Vaccinia Virus Uracil Dna Glycosylase To Be Published.
Page generated: Sat Dec 12 10:46:42 2020

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