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Iron in PDB 1lnb: A Structural Analysis of Metal Substitutions in Thermolysin

Enzymatic activity of A Structural Analysis of Metal Substitutions in Thermolysin

All present enzymatic activity of A Structural Analysis of Metal Substitutions in Thermolysin:
3.4.24.27;

Protein crystallography data

The structure of A Structural Analysis of Metal Substitutions in Thermolysin, PDB code: 1lnb was solved by D.R.Holland, A.C.Hausrath, D.Juers, B.W.Matthews, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.80
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 93.600, 93.600, 131.600, 90.00, 90.00, 120.00
R / Rfree (%) n/a / n/a

Other elements in 1lnb:

The structure of A Structural Analysis of Metal Substitutions in Thermolysin also contains other interesting chemical elements:

Calcium (Ca) 4 atoms

Iron Binding Sites:

The binding sites of Iron atom in the A Structural Analysis of Metal Substitutions in Thermolysin (pdb code 1lnb). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the A Structural Analysis of Metal Substitutions in Thermolysin, PDB code: 1lnb:

Iron binding site 1 out of 1 in 1lnb

Go back to Iron Binding Sites List in 1lnb
Iron binding site 1 out of 1 in the A Structural Analysis of Metal Substitutions in Thermolysin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of A Structural Analysis of Metal Substitutions in Thermolysin within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Fe900

b:11.9
occ:1.00
NE2 E:HIS142 1.9 16.0 1.0
OE2 E:GLU166 1.9 19.3 1.0
NE2 E:HIS146 2.0 12.4 1.0
O E:HOH1479 2.2 17.4 1.0
O E:HOH1480 2.6 21.6 1.0
CD E:GLU166 2.7 13.1 1.0
OE1 E:GLU166 2.9 16.0 1.0
CE1 E:HIS146 2.9 13.5 1.0
CE1 E:HIS142 2.9 14.7 1.0
CD2 E:HIS142 3.0 16.5 1.0
CD2 E:HIS146 3.0 20.9 1.0
OH E:TYR157 3.7 21.0 1.0
ND1 E:HIS146 4.1 15.8 1.0
ND1 E:HIS142 4.1 10.2 1.0
CG E:HIS142 4.1 12.8 1.0
CG E:HIS146 4.1 12.4 1.0
NE2 E:HIS231 4.1 19.4 1.0
CG E:GLU166 4.2 9.6 1.0
CA E:VAL1321 4.2 69.8 1.0
N E:VAL1321 4.4 45.4 1.0
O E:HOH1481 4.4 42.4 1.0
O E:HOH1355 4.5 19.5 1.0
CB E:SER169 4.5 7.6 1.0
OE1 E:GLU143 4.6 14.7 1.0
OG E:SER169 4.7 10.4 1.0
CZ E:TYR157 4.8 24.5 1.0
CD2 E:HIS231 4.8 18.0 1.0
CA E:GLU166 4.8 8.9 1.0
O E:VAL1321 4.9 36.5 1.0
C E:VAL1321 4.9 0.0 1.0
CE1 E:TYR157 5.0 29.6 1.0
OE2 E:GLU143 5.0 22.5 1.0

Reference:

D.R.Holland, A.C.Hausrath, D.Juers, B.W.Matthews. Structural Analysis of Zinc Substitutions in the Active Site of Thermolysin. Protein Sci. V. 4 1955 1995.
ISSN: ISSN 0961-8368
PubMed: 8535232
Page generated: Sun Dec 13 14:22:22 2020

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