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Bromine in PDB 4pod: Structure of Triosephosphate Isomerase I170V Mutant Human Enzyme.

Enzymatic activity of Structure of Triosephosphate Isomerase I170V Mutant Human Enzyme.

All present enzymatic activity of Structure of Triosephosphate Isomerase I170V Mutant Human Enzyme.:
5.3.1.1;

Protein crystallography data

The structure of Structure of Triosephosphate Isomerase I170V Mutant Human Enzyme., PDB code: 4pod was solved by C.G.Amrich, A.A.Aslam, A.Heroux, A.P.Vandemark, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.49 / 1.99
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 63.659, 70.729, 91.749, 90.00, 90.00, 90.00
R / Rfree (%) 17 / 21.3

Other elements in 4pod:

The structure of Structure of Triosephosphate Isomerase I170V Mutant Human Enzyme. also contains other interesting chemical elements:

Potassium (K) 2 atoms
Sodium (Na) 1 atom

Bromine Binding Sites:

The binding sites of Bromine atom in the Structure of Triosephosphate Isomerase I170V Mutant Human Enzyme. (pdb code 4pod). 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 Structure of Triosephosphate Isomerase I170V Mutant Human Enzyme., PDB code: 4pod:

Bromine binding site 1 out of 1 in 4pod

Go back to Bromine Binding Sites List in 4pod
Bromine binding site 1 out of 1 in the Structure of Triosephosphate Isomerase I170V Mutant Human Enzyme.


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Structure of Triosephosphate Isomerase I170V Mutant Human Enzyme. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Br302

b:31.4
occ:1.00
 HE2 B:HIS95 2.4 33.4 1.0
HD22 B:ASN11 2.6 34.3 1.0
OE2 B:GLU165 3.1 35.4 1.0
HG B:LEU230 3.1 31.5 1.0
O2 B:PO4301 3.2 33.4 1.0
HB3 B:ASN11 3.2 29.3 1.0
NE2 B:HIS95 3.2 27.8 1.0
HE3 B:LYS13 3.4 30.5 1.0
ND2 B:ASN11 3.4 28.6 1.0
HA3 B:GLY232 3.5 37.5 1.0
HE2 B:LYS13 3.5 30.5 1.0
HZ3 B:LYS13 3.7 34.9 1.0
HA2 B:GLY232 3.8 37.5 1.0
N B:GLY232 3.8 34.9 1.0
H B:GLY232 3.8 41.8 1.0
OE1 B:GLU165 3.8 32.2 1.0
CE B:LYS13 3.8 25.4 1.0
CD B:GLU165 3.8 34.7 1.0
CA B:GLY232 3.9 31.2 1.0
CB B:ASN11 3.9 24.4 1.0
HB2 B:ASN11 3.9 29.3 1.0
HD21 B:ASN11 4.0 34.3 1.0
CG B:LEU230 4.0 26.3 1.0
HD23 B:LEU230 4.1 31.1 1.0
CD2 B:HIS95 4.1 29.7 1.0
HD21 B:LEU230 4.2 31.1 1.0
CG B:ASN11 4.2 26.3 1.0
CE1 B:HIS95 4.2 29.1 1.0
HD2 B:HIS95 4.2 35.7 1.0
C B:VAL231 4.2 34.5 1.0
HE1 B:HIS95 4.2 34.9 1.0
NZ B:LYS13 4.3 29.0 1.0
HG13 B:VAL170 4.3 36.0 1.0
CD2 B:LEU230 4.3 26.0 1.0
O B:LEU230 4.3 28.0 1.0
P B:PO4301 4.4 34.5 1.0
O3 B:PO4301 4.4 33.1 1.0
C B:LEU230 4.6 33.5 1.0
O B:VAL231 4.7 32.7 1.0
HB3 B:LEU230 4.7 34.9 1.0
HA B:VAL231 4.7 40.9 1.0
N B:VAL231 4.7 35.4 1.0
HD11 B:LEU230 4.7 31.4 1.0
CA B:VAL231 4.8 34.1 1.0
O B:HOH418 4.8 27.6 1.0
HZ1 B:LYS13 4.8 34.9 1.0
HZ2 B:LYS13 4.9 34.9 1.0
CD1 B:LEU230 4.9 26.2 1.0
CB B:LEU230 4.9 29.1 1.0
H B:ASN11 5.0 35.0 1.0

Reference:

B.P.Roland, C.G.Amrich, C.J.Kammerer, K.A.Stuchul, S.B.Larsen, S.Rode, A.A.Aslam, A.Heroux, R.Wetzel, A.P.Vandemark, M.J.Palladino. Triosephosphate Isomerase I170V Alters Catalytic Site, Enhances Stability and Induces Pathology in A Drosophila Model of Tpi Deficiency. Biochim.Biophys.Acta V.1852 61 2015.
ISSN: ISSN 0006-3002
PubMed: 25463631
DOI: 10.1016/J.BBADIS.2014.10.010
Page generated: Mon Jul 7 07:17:15 2025

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