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Bromine in PDB 7z00: Crystal Structure of Vibrio Alkaline Phosphatase in 1.0 M Kbr

Protein crystallography data

The structure of Crystal Structure of Vibrio Alkaline Phosphatase in 1.0 M Kbr, PDB code: 7z00 was solved by S.Markusson, J.G.Hjorleifsson, P.Kursula, B.Asgeirsson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.39 / 2.60
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 99.25, 118.12, 84.4, 90, 90, 90
R / Rfree (%) 24.2 / 29.1

Other elements in 7z00:

The structure of Crystal Structure of Vibrio Alkaline Phosphatase in 1.0 M Kbr also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms
Zinc (Zn) 2 atoms

Bromine Binding Sites:

The binding sites of Bromine atom in the Crystal Structure of Vibrio Alkaline Phosphatase in 1.0 M Kbr (pdb code 7z00). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total only one binding site of Bromine was determined in the Crystal Structure of Vibrio Alkaline Phosphatase in 1.0 M Kbr, PDB code: 7z00:

Bromine binding site 1 out of 1 in 7z00

Go back to Bromine Binding Sites List in 7z00
Bromine binding site 1 out of 1 in the Crystal Structure of Vibrio Alkaline Phosphatase in 1.0 M Kbr


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Crystal Structure of Vibrio Alkaline Phosphatase in 1.0 M Kbr within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Br603

b:92.0
occ:1.00
H B:TYR179 2.5 109.5 1.0
H B:TYR222 2.7 89.7 1.0
HA B:ALA221 3.2 93.6 1.0
HB3 B:TYR179 3.2 111.8 1.0
HA B:VAL178 3.2 111.4 1.0
N B:TYR179 3.3 91.2 1.0
N B:TYR222 3.5 74.7 1.0
HB3 B:TYR222 3.6 93.4 1.0
HB2 B:TYR179 3.6 111.8 1.0
CB B:TYR179 3.8 93.1 1.0
HG13 B:VAL178 3.9 102.3 1.0
HB2 B:TYR222 3.9 93.4 1.0
HG22 B:VAL178 4.0 103.0 1.0
CA B:ALA221 4.0 78.0 1.0
CA B:VAL178 4.1 92.8 1.0
HB1 B:ALA221 4.1 86.8 1.0
CB B:TYR222 4.1 77.8 1.0
C B:VAL178 4.2 94.1 1.0
CA B:TYR179 4.2 93.8 1.0
C B:ALA221 4.3 74.2 1.0
HE21 B:GLN242 4.4 95.3 1.0
CA B:TYR222 4.5 75.0 1.0
CB B:ALA221 4.5 72.2 1.0
HB2 B:ALA221 4.7 86.8 1.0
CG1 B:VAL178 4.7 85.2 1.0
CB B:VAL178 4.7 89.5 1.0
CG2 B:VAL178 4.8 85.8 1.0
HE22 B:GLN242 4.8 95.3 1.0
O B:TYR179 4.9 91.6 1.0
O B:PHE220 4.9 76.8 1.0
HA B:TYR179 4.9 112.6 1.0
O B:ASP177 4.9 99.4 1.0
NE2 B:GLN242 5.0 79.4 1.0
HA B:TYR222 5.0 90.1 1.0

Reference:

S.Markusson, J.G.Hjorleifsson, P.Kursula, B.Asgeirsson. Structural Characterization of Functionally Important Chloride Binding Sites in the Marine Vibrio Alkaline Phosphatase. Biochemistry V. 61 2248 2022.
ISSN: ISSN 0006-2960
PubMed: 36194497
DOI: 10.1021/ACS.BIOCHEM.2C00438
Page generated: Thu Jul 11 04:46:30 2024

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