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Zinc in PDB 6tmn: Structures of Two Thermolysin-Inhibitor Complexes That Differ By A Single Hydrogen Bond

Enzymatic activity of Structures of Two Thermolysin-Inhibitor Complexes That Differ By A Single Hydrogen Bond

All present enzymatic activity of Structures of Two Thermolysin-Inhibitor Complexes That Differ By A Single Hydrogen Bond:
3.4.24.27;

Protein crystallography data

The structure of Structures of Two Thermolysin-Inhibitor Complexes That Differ By A Single Hydrogen Bond, PDB code: 6tmn was solved by D.E.Tronrud, H.M.Holden, B.W.Matthews, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 1.60
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 94.100, 94.100, 131.400, 90.00, 90.00, 120.00
R / Rfree (%) n/a / n/a

Other elements in 6tmn:

The structure of Structures of Two Thermolysin-Inhibitor Complexes That Differ By A Single Hydrogen Bond also contains other interesting chemical elements:

Calcium (Ca) 4 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Structures of Two Thermolysin-Inhibitor Complexes That Differ By A Single Hydrogen Bond (pdb code 6tmn). 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 Structures of Two Thermolysin-Inhibitor Complexes That Differ By A Single Hydrogen Bond, PDB code: 6tmn:

Zinc binding site 1 out of 1 in 6tmn

Go back to Zinc Binding Sites List in 6tmn
Zinc binding site 1 out of 1 in the Structures of Two Thermolysin-Inhibitor Complexes That Differ By A Single Hydrogen Bond


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structures of Two Thermolysin-Inhibitor Complexes That Differ By A Single Hydrogen Bond within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Zn322

b:10.8
occ:1.00
 OE1 E:GLU166 2.0 9.2 1.0
O21 E:0PI317 2.1 9.7 1.0
NE2 E:HIS142 2.1 12.5 1.0
NE2 E:HIS146 2.1 9.7 1.0
CD E:GLU166 2.8 8.7 1.0
OE2 E:GLU166 2.9 6.7 1.0
CE1 E:HIS146 2.9 13.5 1.0
O11 E:0PI317 3.0 11.4 1.0
P E:0PI317 3.0 11.3 1.0
CE1 E:HIS142 3.1 6.7 1.0
CD2 E:HIS142 3.1 4.8 1.0
CD2 E:HIS146 3.2 9.4 1.0
OH E:TYR157 3.8 11.6 1.0
OS E:0PI317 4.0 5.0 1.0
NE2 E:HIS231 4.1 5.5 1.0
ND1 E:HIS146 4.1 8.7 1.0
CA E:0PI317 4.2 11.6 1.0
ND1 E:HIS142 4.2 5.5 1.0
CG E:HIS142 4.2 7.9 1.0
CG E:GLU166 4.2 6.5 1.0
CG E:HIS146 4.3 10.6 1.0
CB E:SER169 4.5 3.9 1.0
N E:0PI317 4.6 13.1 1.0
C E:0PI317 4.6 6.8 1.0
C9 E:0PI317 4.6 18.6 1.0
CD2 E:HIS231 4.6 10.2 1.0
O E:HOH487 4.7 9.9 1.0
O E:0PI317 4.7 10.6 1.0
CZ E:TYR157 4.7 11.2 1.0
CA E:GLU166 4.8 4.5 1.0
OG E:SER169 4.8 6.9 1.0
CE2 E:TYR157 4.8 17.0 1.0
OE2 E:GLU143 5.0 14.0 1.0

Reference:

D.E.Tronrud, H.M.Holden, B.W.Matthews. Structures of Two Thermolysin-Inhibitor Complexes That Differ By A Single Hydrogen Bond. Science V. 235 571 1987.
ISSN: ISSN 0036-8075
PubMed: 3810156
Page generated: Tue Oct 29 08:07:22 2024

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