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Zinc in PDB 1lu0: Atomic Resolution Structure of Squash Trypsin Inhibitor: Unexpected Metal Coordination

Protein crystallography data

The structure of Atomic Resolution Structure of Squash Trypsin Inhibitor: Unexpected Metal Coordination, PDB code: 1lu0 was solved by R.Thaimattam, E.Tykarska, A.Bierzynski, G.M.Sheldrick, M.Jaskolski, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.03
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 47.280, 58.630, 19.320, 90.00, 90.00, 90.00
R / Rfree (%) 12 / 14.5

Zinc Binding Sites:

The binding sites of Zinc atom in the Atomic Resolution Structure of Squash Trypsin Inhibitor: Unexpected Metal Coordination (pdb code 1lu0). 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 Atomic Resolution Structure of Squash Trypsin Inhibitor: Unexpected Metal Coordination, PDB code: 1lu0:

Zinc binding site 1 out of 1 in 1lu0

Go back to Zinc Binding Sites List in 1lu0
Zinc binding site 1 out of 1 in the Atomic Resolution Structure of Squash Trypsin Inhibitor: Unexpected Metal Coordination


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Atomic Resolution Structure of Squash Trypsin Inhibitor: Unexpected Metal Coordination within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn201

b:8.6
occ:0.50
OE1 A:GLU19 2.0 9.8 1.0
OE2 B:GLU19 2.0 9.2 1.0
CD B:GLU19 2.7 8.8 1.0
CD A:GLU19 2.7 8.9 1.0
OE1 B:GLU19 2.7 8.8 1.0
OE2 A:GLU19 2.8 10.2 1.0
CG B:GLU19 4.1 8.7 1.0
O B:HOH347 4.1 13.5 0.7
CG A:GLU19 4.2 9.7 1.0
O A:HOH303 4.3 12.8 1.0
O1 B:SO4205 4.3 17.9 0.3
CA B:ARG1 4.8 9.9 1.0
S B:SO4205 4.9 13.5 0.2
N B:VAL2 5.0 9.6 1.0

Reference:

R.Thaimattam, E.Tykarska, A.Bierzynski, G.M.Sheldrick, M.Jaskolski. Atomic Resolution Structure of Squash Trypsin Inhibitor: Unexpected Metal Coordination. Acta Crystallogr.,Sect.D V. 58 1448 2002.
ISSN: ISSN 0907-4449
PubMed: 12198301
DOI: 10.1107/S0907444902011769
Page generated: Sun Oct 13 05:14:00 2024

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