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Zinc in PDB 5n12: Crystal Structure of Tce Treated Rppep-1

Enzymatic activity of Crystal Structure of Tce Treated Rppep-1

All present enzymatic activity of Crystal Structure of Tce Treated Rppep-1:
3.4.24.89;

Protein crystallography data

The structure of Crystal Structure of Tce Treated Rppep-1, PDB code: 5n12 was solved by C.Pichlo, M.Schacherl, U.Baumann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.53 / 1.38
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 43.169, 71.769, 117.798, 90.00, 90.00, 90.00
R / Rfree (%) 16.4 / 18.4

Other elements in 5n12:

The structure of Crystal Structure of Tce Treated Rppep-1 also contains other interesting chemical elements:

Chlorine (Cl) 9 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Tce Treated Rppep-1 (pdb code 5n12). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Tce Treated Rppep-1, PDB code: 5n12:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 5n12

Go back to Zinc Binding Sites List in 5n12
Zinc binding site 1 out of 2 in the Crystal Structure of Tce Treated Rppep-1


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 Tce Treated Rppep-1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:14.1
occ:1.00
OE1 A:GLU185 2.1 12.1 1.0
NE2 A:HIS142 2.1 11.2 1.0
NE2 A:HIS146 2.1 11.3 1.0
N A:TRS303 2.1 16.1 1.0
O2 A:TRS303 2.2 16.0 1.0
O3 A:TRS303 2.3 18.1 1.0
HO3 A:TRS303 2.4 21.8 1.0
HO2 A:TRS303 2.5 19.2 1.0
HN1 A:TRS303 2.5 19.3 1.0
HN2 A:TRS303 2.6 19.3 1.0
C A:TRS303 2.9 16.5 1.0
CD A:GLU185 3.0 13.5 1.0
C2 A:TRS303 3.0 15.8 1.0
CD2 A:HIS142 3.0 11.6 1.0
CD2 A:HIS146 3.1 10.6 1.0
CE1 A:HIS146 3.1 11.9 1.0
CE1 A:HIS142 3.1 10.4 1.0
C3 A:TRS303 3.1 17.8 1.0
OE2 A:GLU185 3.2 14.1 1.0
HD2 A:HIS142 3.2 14.0 1.0
HD2 A:HIS146 3.2 12.8 1.0
HE1 A:HIS146 3.3 14.3 1.0
HE1 A:HIS142 3.3 12.4 1.0
H22 A:TRS303 3.4 18.9 1.0
H32 A:TRS303 3.7 21.4 1.0
H31 A:TRS303 3.8 21.4 1.0
H21 A:TRS303 3.9 18.9 1.0
HA A:GLU185 4.1 13.1 1.0
ND1 A:HIS146 4.2 11.7 1.0
ND1 A:HIS142 4.2 10.8 1.0
CG A:HIS142 4.2 11.2 1.0
OH A:TYR178 4.2 16.8 1.0
CG A:HIS146 4.2 10.8 1.0
O A:HOH501 4.2 19.5 1.0
OE1 A:GLU143 4.3 13.0 1.0
HB3 A:ALA188 4.3 14.5 1.0
O A:HOH578 4.3 13.5 1.0
C1 A:TRS303 4.3 18.0 1.0
CG A:GLU185 4.4 13.0 1.0
HE2 A:TYR178 4.4 21.0 1.0
HB3 A:GLU185 4.5 13.9 1.0
H11 A:TRS303 4.6 21.6 1.0
HH A:TYR178 4.7 20.1 1.0
HB1 A:ALA188 4.8 14.5 1.0
HG3 A:GLU185 4.8 15.7 1.0
CB A:GLU185 4.8 11.6 1.0
CB A:ALA188 4.8 12.1 1.0
OE2 A:GLU143 4.9 17.5 1.0
HB2 A:ALA188 4.9 14.5 1.0
H12 A:TRS303 4.9 21.6 1.0
CA A:GLU185 4.9 10.9 1.0
HG2 A:GLU185 5.0 15.7 1.0
HD1 A:HIS146 5.0 14.0 1.0
CD A:GLU143 5.0 14.0 1.0
O1 A:TRS303 5.0 16.9 1.0
HD1 A:HIS142 5.0 13.0 1.0

Zinc binding site 2 out of 2 in 5n12

Go back to Zinc Binding Sites List in 5n12
Zinc binding site 2 out of 2 in the Crystal Structure of Tce Treated Rppep-1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Tce Treated Rppep-1 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn301

b:13.8
occ:1.00
HO2 B:TRS304 1.6 30.3 1.0
HO3 B:TRS304 2.0 28.1 1.0
OE1 B:GLU185 2.0 14.9 1.0
NE2 B:HIS146 2.1 11.1 1.0
NE2 B:HIS142 2.1 11.9 1.0
N B:TRS304 2.1 25.7 1.0
O2 B:TRS304 2.2 25.2 1.0
O3 B:TRS304 2.4 23.5 1.0
HN2 B:TRS304 2.5 30.9 1.0
HN1 B:TRS304 2.6 30.9 1.0
C B:TRS304 2.9 27.6 1.0
CD B:GLU185 2.9 14.8 1.0
CE1 B:HIS146 3.0 11.3 1.0
CD2 B:HIS142 3.0 10.8 1.0
C2 B:TRS304 3.0 27.1 1.0
CE1 B:HIS142 3.1 11.5 1.0
CD2 B:HIS146 3.1 11.2 1.0
HE1 B:HIS146 3.2 13.6 1.0
HD2 B:HIS142 3.2 13.0 1.0
OE2 B:GLU185 3.2 16.7 1.0
C3 B:TRS304 3.2 24.7 1.0
HE1 B:HIS142 3.3 13.8 1.0
HD2 B:HIS146 3.3 13.5 1.0
H22 B:TRS304 3.5 32.5 1.0
H32 B:TRS304 3.8 29.6 1.0
H21 B:TRS304 3.8 32.5 1.0
H31 B:TRS304 3.9 29.6 1.0
HA B:GLU185 4.0 14.1 1.0
ND1 B:HIS146 4.1 12.0 1.0
HB3 B:ALA188 4.2 14.5 1.0
ND1 B:HIS142 4.2 11.7 1.0
CG B:HIS142 4.2 11.2 1.0
CG B:HIS146 4.2 10.8 1.0
OE1 B:GLU143 4.2 14.0 1.0
C1 B:TRS304 4.3 32.0 1.0
CG B:GLU185 4.3 13.2 1.0
O B:HOH566 4.3 17.8 1.0
OH B:TYR178 4.4 20.4 1.0
O B:HOH534 4.4 18.8 1.0
HE2 B:TYR178 4.4 22.9 1.0
HB3 B:GLU185 4.5 15.0 1.0
H11 B:TRS304 4.5 38.4 1.0
H12 B:TRS304 4.6 38.4 1.0
HB1 B:ALA188 4.7 14.5 1.0
HG3 B:GLU185 4.7 15.9 1.0
CB B:ALA188 4.8 12.1 1.0
CB B:GLU185 4.8 12.5 1.0
OE2 B:GLU143 4.8 20.5 1.0
CA B:GLU185 4.8 11.8 1.0
HB2 B:ALA188 4.8 14.5 1.0
HH B:TYR178 4.9 24.4 1.0
HG2 B:GLU185 4.9 15.9 1.0
CD B:GLU143 4.9 15.6 1.0
HD1 B:HIS146 4.9 14.3 1.0
HD1 B:HIS142 5.0 14.0 1.0

Reference:

C.Pichlo, C.Toelzer, K.Chojnacki, S.Ocal, M.Uthoff, S.Ruegenberg, T.Hermanns, M.Schacherl, M.S.Denzel, K.Hofmann, K.Niefind, U.Baumann. Improved Protein-Crystal Identification By Using 2,2,2-Trichloroethanol As A Fluorescence Enhancer. Acta Crystallogr F Struct V. 74 307 2018BIOL Commun.
ISSN: ESSN 2053-230X
PubMed: 29717999
DOI: 10.1107/S2053230X18005253
Page generated: Wed Dec 16 06:34:07 2020

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