Atomistry » Zinc » PDB 4rvh-4tpg » 4to8
Atomistry »
  Zinc »
    PDB 4rvh-4tpg »
      4to8 »

Zinc in PDB 4to8: Methicillin-Resistant Staphylococcus Aureus Class Iib Fructose 1,6- Bisphosphate Aldolase

Enzymatic activity of Methicillin-Resistant Staphylococcus Aureus Class Iib Fructose 1,6- Bisphosphate Aldolase

All present enzymatic activity of Methicillin-Resistant Staphylococcus Aureus Class Iib Fructose 1,6- Bisphosphate Aldolase:
4.1.2.13;

Protein crystallography data

The structure of Methicillin-Resistant Staphylococcus Aureus Class Iib Fructose 1,6- Bisphosphate Aldolase, PDB code: 4to8 was solved by G.C.Capodagli, S.D.Pegan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 51.50 / 2.10
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 76.464, 96.054, 101.231, 90.00, 90.00, 90.00
R / Rfree (%) 17.6 / 22.8

Zinc Binding Sites:

The binding sites of Zinc atom in the Methicillin-Resistant Staphylococcus Aureus Class Iib Fructose 1,6- Bisphosphate Aldolase (pdb code 4to8). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Methicillin-Resistant Staphylococcus Aureus Class Iib Fructose 1,6- Bisphosphate Aldolase, PDB code: 4to8:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 4to8

Go back to Zinc Binding Sites List in 4to8
Zinc binding site 1 out of 2 in the Methicillin-Resistant Staphylococcus Aureus Class Iib Fructose 1,6- Bisphosphate Aldolase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Methicillin-Resistant Staphylococcus Aureus Class Iib Fructose 1,6- Bisphosphate Aldolase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:20.1
occ:1.00
ND1 A:HIS209 2.1 14.9 1.0
OB1 A:FLC302 2.1 21.4 1.0
NE2 A:HIS86 2.1 18.4 1.0
OG2 A:FLC302 2.1 21.1 1.0
OHB A:FLC302 2.1 17.2 1.0
O A:HOH514 2.2 16.1 1.0
CBC A:FLC302 2.9 24.8 1.0
CB A:FLC302 3.0 25.2 1.0
CE1 A:HIS209 3.0 14.6 1.0
CE1 A:HIS86 3.0 15.3 1.0
CG A:HIS209 3.2 17.3 1.0
CD2 A:HIS86 3.2 14.3 1.0
CGC A:FLC302 3.2 20.6 1.0
CB A:HIS209 3.6 14.0 1.0
CG A:FLC302 3.6 25.0 1.0
OB2 A:FLC302 4.1 24.0 1.0
NE2 A:HIS209 4.1 16.4 1.0
ND1 A:HIS86 4.2 11.7 1.0
CD2 A:HIS209 4.2 14.3 1.0
CG A:HIS86 4.3 17.1 1.0
ND2 A:ASN231 4.3 17.6 1.0
OG1 A:FLC302 4.3 23.4 1.0
CA A:FLC302 4.3 32.3 1.0
O A:HOH472 4.5 18.7 1.0
O A:HOH494 4.5 19.2 1.0
CA A:HIS209 4.5 17.1 1.0
OD1 A:ASP85 4.6 16.5 1.0
OA2 A:FLC302 4.6 31.6 1.0
OD2 A:ASP85 4.7 18.2 1.0
CAC A:FLC302 4.9 31.2 1.0
N A:GLY210 5.0 18.7 1.0

Zinc binding site 2 out of 2 in 4to8

Go back to Zinc Binding Sites List in 4to8
Zinc binding site 2 out of 2 in the Methicillin-Resistant Staphylococcus Aureus Class Iib Fructose 1,6- Bisphosphate Aldolase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Methicillin-Resistant Staphylococcus Aureus Class Iib Fructose 1,6- Bisphosphate Aldolase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn301

b:17.6
occ:1.00
OG1 B:FLC302 2.1 18.9 1.0
ND1 B:HIS209 2.1 12.9 1.0
OB2 B:FLC302 2.1 17.4 1.0
NE2 B:HIS86 2.1 15.1 1.0
OHB B:FLC302 2.1 19.5 1.0
O B:HOH491 2.2 12.2 1.0
CBC B:FLC302 2.9 24.8 1.0
CE1 B:HIS209 2.9 11.9 1.0
CB B:FLC302 3.0 24.9 1.0
CE1 B:HIS86 3.1 12.4 1.0
CGC B:FLC302 3.1 19.2 1.0
CD2 B:HIS86 3.2 13.7 1.0
CG B:HIS209 3.2 13.6 1.0
CG B:FLC302 3.6 21.6 1.0
CB B:HIS209 3.6 11.3 1.0
NE2 B:HIS209 4.1 11.2 1.0
OB1 B:FLC302 4.1 25.0 1.0
ND1 B:HIS86 4.2 12.4 1.0
OG2 B:FLC302 4.2 25.0 1.0
ND2 B:ASN231 4.2 13.5 1.0
CD2 B:HIS209 4.3 12.8 1.0
CG B:HIS86 4.3 16.4 1.0
CA B:FLC302 4.4 29.7 1.0
O B:HOH527 4.4 17.3 1.0
O B:HOH486 4.4 16.2 1.0
OA1 B:FLC302 4.5 28.8 1.0
CA B:HIS209 4.5 15.3 1.0
OD1 B:ASP85 4.6 11.6 1.0
OD2 B:ASP85 4.6 20.4 1.0
CAC B:FLC302 4.9 31.8 1.0
N B:GLY210 5.0 15.3 1.0

Reference:

G.C.Capodagli, S.A.Lee, K.J.Boehm, K.M.Brady, S.D.Pegan. Structural and Functional Characterization of Methicillin-Resistant Staphylococcus Aureus'S Class Iib Fructose 1,6-Bisphosphate Aldolase. Biochemistry 2014.
ISSN: ISSN 0006-2960
PubMed: 25390935
DOI: 10.1021/BI501141T
Page generated: Wed Dec 16 05:47:05 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