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Zinc in PDB 1pm5: Crystal Structure of Wild Type Lactococcus Lactis Fpg Complexed to A Tetrahydrofuran Containing Dna

Enzymatic activity of Crystal Structure of Wild Type Lactococcus Lactis Fpg Complexed to A Tetrahydrofuran Containing Dna

All present enzymatic activity of Crystal Structure of Wild Type Lactococcus Lactis Fpg Complexed to A Tetrahydrofuran Containing Dna:
3.2.2.23;

Protein crystallography data

The structure of Crystal Structure of Wild Type Lactococcus Lactis Fpg Complexed to A Tetrahydrofuran Containing Dna, PDB code: 1pm5 was solved by K.Pereira De Jesus-Tran, L.Serre, C.Zelwer, B.Castaing, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.95
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 91.784, 91.784, 141.792, 90.00, 90.00, 90.00
R / Rfree (%) 19.6 / 21.6

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Wild Type Lactococcus Lactis Fpg Complexed to A Tetrahydrofuran Containing Dna (pdb code 1pm5). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of Wild Type Lactococcus Lactis Fpg Complexed to A Tetrahydrofuran Containing Dna, PDB code: 1pm5:

Zinc binding site 1 out of 1 in 1pm5

Go back to Zinc Binding Sites List in 1pm5
Zinc binding site 1 out of 1 in the Crystal Structure of Wild Type Lactococcus Lactis Fpg Complexed to A Tetrahydrofuran Containing Dna


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Wild Type Lactococcus Lactis Fpg Complexed to A Tetrahydrofuran Containing Dna within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn300

b:28.8
occ:1.00
 SG A:CYS265 2.2 25.1 1.0
SG A:CYS268 2.4 27.8 1.0
SG A:CYS245 2.4 26.8 1.0
SG A:CYS248 2.5 28.5 1.0
CB A:CYS245 3.1 29.3 1.0
CB A:CYS268 3.3 28.4 1.0
CB A:CYS265 3.4 24.0 1.0
CB A:CYS248 3.4 32.2 1.0
N A:CYS268 3.8 26.2 1.0
N A:CYS248 3.8 33.6 1.0
CA A:CYS268 4.1 27.4 1.0
CA A:CYS248 4.2 33.7 1.0
CB A:VAL267 4.4 24.5 1.0
NE1 A:TRP179 4.5 22.4 1.0
CB A:ARG247 4.6 34.5 1.0
CA A:CYS245 4.6 30.8 1.0
CA A:CYS265 4.8 24.7 1.0
N A:GLY249 4.8 33.9 1.0
CB A:ALA250 4.8 29.3 1.0
C A:VAL267 4.8 26.6 1.0
C A:ARG247 4.8 34.7 1.0
C A:CYS248 4.8 34.5 1.0
N A:ALA250 4.9 29.9 1.0
NE A:ARG247 4.9 33.2 1.0
CG1 A:VAL267 4.9 25.1 1.0

Reference:

K.Pereira De Jesus, L.Serre, C.Zelwer, B.Castaing. Structural Insights Into Abasic Site For Fpg Specific Binding and Catalysis: Comparative High-Resolution Crystallographic Studies of Fpg Bound to Various Models of Abasic Site Analogues-Containing Dna. Nucleic Acids Res. V. 33 5936 2005.
ISSN: ISSN 0305-1048
PubMed: 16243784
DOI: 10.1093/NAR/GKI879
Page generated: Wed Oct 16 17:51:26 2024

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