Chlorine in PDB 5zi2: MDH3 Wild Type, Nad-Form

Enzymatic activity of MDH3 Wild Type, Nad-Form

All present enzymatic activity of MDH3 Wild Type, Nad-Form:
1.1.1.37;

Protein crystallography data

The structure of MDH3 Wild Type, Nad-Form, PDB code: 5zi2 was solved by S.Moriyama, K.Nishio, T.Mizushima, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.00
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 45.099, 92.559, 82.114, 90.00, 99.88, 90.00
R / Rfree (%) 17.5 / 23

Chlorine Binding Sites:

The binding sites of Chlorine atom in the MDH3 Wild Type, Nad-Form (pdb code 5zi2). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the MDH3 Wild Type, Nad-Form, PDB code: 5zi2:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 5zi2

Go back to Chlorine Binding Sites List in 5zi2
Chlorine binding site 1 out of 2 in the MDH3 Wild Type, Nad-Form


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of MDH3 Wild Type, Nad-Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl403

b:26.3
occ:1.00
O A:HOH557 3.2 19.0 1.0
ND2 A:ASN110 3.3 20.0 1.0
N A:ASN110 3.5 19.9 1.0
CA A:ALA108 3.6 22.6 1.0
CB A:ASN110 3.6 20.4 1.0
C A:ALA108 3.6 22.3 1.0
N A:PRO109 3.7 21.6 1.0
CD A:PRO109 3.7 22.7 1.0
CG A:ASN110 3.9 21.5 1.0
CA A:ASN110 4.1 20.7 1.0
CB A:ALA108 4.3 22.3 1.0
O A:ALA108 4.3 19.9 1.0
CG A:PRO109 4.4 22.9 1.0
C A:PRO109 4.5 19.4 1.0
CA A:PRO109 4.6 20.6 1.0
O A:PHE107 4.7 24.4 1.0
C A:ASN110 4.7 22.2 1.0
N A:ALA111 4.8 19.2 1.0
N A:ALA108 4.8 22.3 1.0

Chlorine binding site 2 out of 2 in 5zi2

Go back to Chlorine Binding Sites List in 5zi2
Chlorine binding site 2 out of 2 in the MDH3 Wild Type, Nad-Form


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of MDH3 Wild Type, Nad-Form within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl401

b:27.2
occ:1.00
ND2 B:ASN110 3.2 25.3 1.0
O B:HOH533 3.2 25.8 1.0
O B:HOH547 3.3 26.3 1.0
N B:ASN110 3.5 20.9 1.0
CA B:ALA108 3.5 23.5 1.0
C B:ALA108 3.6 24.2 1.0
CB B:ASN110 3.7 21.6 1.0
N B:PRO109 3.7 23.8 1.0
CD B:PRO109 3.8 24.5 1.0
CG B:ASN110 3.9 25.6 1.0
CA B:ASN110 4.1 22.1 1.0
CB B:ALA108 4.1 24.8 1.0
O B:ALA108 4.3 24.3 1.0
CG B:PRO109 4.4 24.6 1.0
C B:PRO109 4.5 21.4 1.0
CA B:PRO109 4.6 23.1 1.0
N B:ALA108 4.7 23.9 1.0
O B:PHE107 4.7 24.2 1.0
C B:ASN110 4.8 23.7 1.0
N B:ALA111 4.8 21.5 1.0
O B:HOH577 4.9 33.9 1.0
O B:ALA69 4.9 24.3 1.0

Reference:

S.Moriyama, K.Nishio, T.Mizushima. Structure of Glyoxysomal Malate Dehydrogenase (MDH3) From Saccharomyces Cerevisiae. Acta Crystallogr F Struct V. 74 617 2018BIOL Commun.
ISSN: ESSN 2053-230X
PubMed: 30279312
DOI: 10.1107/S2053230X18011895
Page generated: Sat Dec 12 12:42:14 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy