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Manganese in PDB 3r7p: The Crystal Structure of I-Ltri

Enzymatic activity of The Crystal Structure of I-Ltri

All present enzymatic activity of The Crystal Structure of I-Ltri:
3.1.21.1;

Protein crystallography data

The structure of The Crystal Structure of I-Ltri, PDB code: 3r7p was solved by A.N.S.Mak, R.Takeuchi, D.R.Edgell, B.L.Stoddard, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.29 / 2.70
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 113.089, 42.595, 103.195, 90.00, 110.63, 90.00
R / Rfree (%) 19.2 / 27

Other elements in 3r7p:

The structure of The Crystal Structure of I-Ltri also contains other interesting chemical elements:

Magnesium (Mg) 4 atoms

Manganese Binding Sites:

The binding sites of Manganese atom in the The Crystal Structure of I-Ltri (pdb code 3r7p). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the The Crystal Structure of I-Ltri, PDB code: 3r7p:

Manganese binding site 1 out of 1 in 3r7p

Go back to Manganese Binding Sites List in 3r7p
Manganese binding site 1 out of 1 in the The Crystal Structure of I-Ltri


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of The Crystal Structure of I-Ltri within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn316

b:42.4
occ:1.00
OP2 C:DA17 2.0 40.8 1.0
OE2 A:GLU29 2.1 41.8 1.0
OP3 E:DG16 2.1 43.6 1.0
OE1 A:GLU184 2.1 46.9 1.0
OE1 A:GLU29 2.4 39.6 1.0
OP3 C:DA17 2.6 39.2 1.0
CD A:GLU29 2.6 40.0 1.0
P C:DA17 2.8 40.6 1.0
CD A:GLU184 3.0 46.5 1.0
O3' D:DC15 3.2 44.0 1.0
P E:DG16 3.4 46.2 1.0
OE2 A:GLU184 3.4 47.6 1.0
MG A:MG317 3.6 29.3 1.0
O5' C:DA17 3.7 39.6 1.0
OP1 E:DG16 3.8 45.5 1.0
MG E:MG2 3.8 31.4 1.0
O5' E:DG16 3.8 46.0 1.0
O A:ALA28 3.9 38.3 1.0
O A:GLY183 3.9 41.5 1.0
O E:HOH28 4.0 36.3 1.0
OP1 C:DA17 4.0 40.9 1.0
C A:GLY183 4.1 41.3 1.0
CG A:GLU29 4.1 38.8 1.0
C3' D:DC15 4.1 44.0 1.0
C4' B:DT16 4.2 51.0 1.0
CG A:GLU184 4.2 43.5 1.0
N A:GLU184 4.4 41.1 1.0
C5' B:DT16 4.4 51.1 1.0
C4' D:DC15 4.4 43.6 1.0
CA A:GLU184 4.4 41.4 1.0
C A:ALA28 4.5 38.0 1.0
OP2 E:DG16 4.5 45.1 1.0
C5' C:DA17 4.6 40.0 1.0
CA A:GLY183 4.6 41.2 1.0
OP1 D:DC15 4.8 41.5 1.0
CB A:GLU184 4.8 41.5 1.0
CB A:ALA28 4.8 38.0 1.0
C5' D:DC15 4.9 44.1 1.0
O D:HOH22 4.9 41.7 1.0
O3' B:DT16 4.9 51.7 1.0
CA A:GLU29 4.9 38.1 1.0
O A:HOH323 4.9 27.2 1.0
CB A:GLU29 5.0 38.1 1.0

Reference:

R.Takeuchi, A.R.Lambert, A.N.Mak, K.Jacoby, R.J.Dickson, G.B.Gloor, A.M.Scharenberg, D.R.Edgell, B.L.Stoddard. Tapping Natural Reservoirs of Homing Endonucleases For Targeted Gene Modification. Proc.Natl.Acad.Sci.Usa V. 108 13077 2011.
ISSN: ISSN 0027-8424
PubMed: 21784983
DOI: 10.1073/PNAS.1107719108
Page generated: Tue Dec 15 04:14:37 2020

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