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Zinc in PDB 5k7t: Microed Structure of Thermolysin at 2.5 A Resolution

Enzymatic activity of Microed Structure of Thermolysin at 2.5 A Resolution

All present enzymatic activity of Microed Structure of Thermolysin at 2.5 A Resolution:
3.4.24.27;

Other elements in 5k7t:

The structure of Microed Structure of Thermolysin at 2.5 A Resolution also contains other interesting chemical elements:

Calcium (Ca) 4 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Microed Structure of Thermolysin at 2.5 A Resolution (pdb code 5k7t). 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 Microed Structure of Thermolysin at 2.5 A Resolution, PDB code: 5k7t:

Zinc binding site 1 out of 1 in 5k7t

Go back to Zinc Binding Sites List in 5k7t
Zinc binding site 1 out of 1 in the Microed Structure of Thermolysin at 2.5 A Resolution


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Microed Structure of Thermolysin at 2.5 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn605

b:4.5
occ:1.00
OE2 A:GLU398 2.0 5.0 1.0
NE2 A:HIS378 2.2 4.3 1.0
NE2 A:HIS374 2.2 4.1 1.0
CE1 A:HIS378 2.8 4.4 1.0
CD A:GLU398 2.9 6.5 1.0
CE1 A:HIS374 2.9 4.5 1.0
OE1 A:GLU398 3.1 6.6 1.0
CD2 A:HIS378 3.3 4.1 1.0
CD2 A:HIS374 3.3 3.8 1.0
O A:HOH716 3.4 3.6 1.0
OE2 A:GLU375 3.5 4.0 1.0
OH A:TYR389 3.6 6.4 1.0
ND1 A:HIS378 4.0 4.8 1.0
CD A:GLU375 4.0 4.5 1.0
OE1 A:GLU375 4.0 4.3 1.0
ND1 A:HIS374 4.1 4.6 1.0
CG A:HIS378 4.2 4.4 1.0
CG A:HIS374 4.3 4.4 1.0
CG A:GLU398 4.3 6.3 1.0
O2 A:IPA607 4.5 4.1 1.0
NE2 A:HIS463 4.6 7.5 1.0
CB A:SER401 4.6 3.7 1.0
CZ A:TYR389 4.8 8.4 1.0
OG A:SER401 4.8 3.8 1.0
CA A:GLU398 4.8 4.1 1.0

Reference:

M.J.De La Cruz, J.Hattne, D.Shi, P.Seidler, J.Rodriguez, F.E.Reyes, M.R.Sawaya, D.Cascio, S.C.Weiss, S.K.Kim, C.S.Hinck, A.P.Hinck, G.Calero, D.Eisenberg, T.Gonen. Atomic-Resolution Structures From Fragmented Protein Crystals with the Cryoem Method Microed. Nat. Methods V. 14 399 2017.
ISSN: ESSN 1548-7105
PubMed: 28192420
DOI: 10.1038/NMETH.4178
Page generated: Sun Oct 27 20:08:43 2024

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