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Zinc in PDB 4niy: Crystal Structure of Trypsiligase (K60E/N143H/Y151H/D189K Trypsin) Complexed to Yrh-Ecotin (M84Y/M85R/A86H Ecotin)

Enzymatic activity of Crystal Structure of Trypsiligase (K60E/N143H/Y151H/D189K Trypsin) Complexed to Yrh-Ecotin (M84Y/M85R/A86H Ecotin)

All present enzymatic activity of Crystal Structure of Trypsiligase (K60E/N143H/Y151H/D189K Trypsin) Complexed to Yrh-Ecotin (M84Y/M85R/A86H Ecotin):
3.4.21.4;

Protein crystallography data

The structure of Crystal Structure of Trypsiligase (K60E/N143H/Y151H/D189K Trypsin) Complexed to Yrh-Ecotin (M84Y/M85R/A86H Ecotin), PDB code: 4niy was solved by M.Schoepfel, C.Parthier, M.T.Stubbs, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.60 / 2.84
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 94.241, 78.615, 98.084, 90.00, 96.62, 90.00
R / Rfree (%) 19.2 / 25.2

Other elements in 4niy:

The structure of Crystal Structure of Trypsiligase (K60E/N143H/Y151H/D189K Trypsin) Complexed to Yrh-Ecotin (M84Y/M85R/A86H Ecotin) also contains other interesting chemical elements:

Calcium (Ca) 4 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Trypsiligase (K60E/N143H/Y151H/D189K Trypsin) Complexed to Yrh-Ecotin (M84Y/M85R/A86H Ecotin) (pdb code 4niy). 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 Crystal Structure of Trypsiligase (K60E/N143H/Y151H/D189K Trypsin) Complexed to Yrh-Ecotin (M84Y/M85R/A86H Ecotin), PDB code: 4niy:

Zinc binding site 1 out of 1 in 4niy

Go back to Zinc Binding Sites List in 4niy
Zinc binding site 1 out of 1 in the Crystal Structure of Trypsiligase (K60E/N143H/Y151H/D189K Trypsin) Complexed to Yrh-Ecotin (M84Y/M85R/A86H Ecotin)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Trypsiligase (K60E/N143H/Y151H/D189K Trypsin) Complexed to Yrh-Ecotin (M84Y/M85R/A86H Ecotin) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn302

b:81.2
occ:1.00
 NE2 B:HIS143 2.4 58.9 1.0
NE2 F:HIS86 2.4 55.0 1.0
ND1 B:HIS151 3.1 56.8 1.0
CD2 F:HIS86 3.1 44.9 1.0
CE1 B:HIS151 3.3 58.8 1.0
CE1 B:HIS143 3.3 55.1 1.0
CD2 B:HIS143 3.3 52.6 1.0
CE1 F:HIS86 3.6 41.7 1.0
CG B:HIS151 4.3 52.8 1.0
CG F:HIS86 4.4 40.9 1.0
ND1 B:HIS143 4.4 50.5 1.0
CG B:HIS143 4.5 47.1 1.0
NE2 B:HIS151 4.5 58.4 1.0
ND1 F:HIS86 4.6 45.6 1.0

Reference:

S.Liebscher, M.Schopfel, T.Aumuller, A.Sharkhuukhen, A.Pech, E.Hoss, C.Parthier, G.Jahreis, M.T.Stubbs, F.Bordusa. N-Terminal Protein Modification By Substrate-Activated Reverse Proteolysis. Angew.Chem.Int.Ed.Engl. V. 53 3024 2014.
ISSN: ISSN 1433-7851
PubMed: 24520050
DOI: 10.1002/ANIE.201307736
Page generated: Wed Dec 16 05:37:15 2020

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