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Zinc in PDB 2b44: Truncated S. Aureus Lytm, P 32 2 1 Crystal Form

Enzymatic activity of Truncated S. Aureus Lytm, P 32 2 1 Crystal Form

All present enzymatic activity of Truncated S. Aureus Lytm, P 32 2 1 Crystal Form:
3.4.24.75;

Protein crystallography data

The structure of Truncated S. Aureus Lytm, P 32 2 1 Crystal Form, PDB code: 2b44 was solved by M.Firczuk, A.Mucha, M.Bochtler, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.25 / 1.83
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 100.434, 100.434, 103.038, 90.00, 90.00, 120.00
R / Rfree (%) 18.1 / 19.3

Zinc Binding Sites:

The binding sites of Zinc atom in the Truncated S. Aureus Lytm, P 32 2 1 Crystal Form (pdb code 2b44). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Truncated S. Aureus Lytm, P 32 2 1 Crystal Form, PDB code: 2b44:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 2b44

Go back to Zinc Binding Sites List in 2b44
Zinc binding site 1 out of 2 in the Truncated S. Aureus Lytm, P 32 2 1 Crystal Form


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Truncated S. Aureus Lytm, P 32 2 1 Crystal Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn400

b:27.6
occ:1.00
OD1 A:ASP214 2.0 24.3 1.0
ND1 A:HIS293 2.0 23.0 1.0
O4 A:PO4500 2.0 28.0 1.0
NE2 A:HIS210 2.0 20.5 0.5
NE2 A:HIS210 2.1 21.1 0.5
CG A:ASP214 2.8 25.9 1.0
CE1 A:HIS293 2.9 25.1 1.0
OD2 A:ASP214 3.0 30.5 1.0
CD2 A:HIS210 3.0 23.5 0.5
CE1 A:HIS210 3.0 22.8 0.5
CD2 A:HIS210 3.0 24.1 0.5
CE1 A:HIS210 3.0 23.7 0.5
P A:PO4500 3.1 28.4 1.0
CG A:HIS293 3.1 23.2 1.0
O3 A:PO4500 3.2 27.9 1.0
CB A:HIS293 3.5 23.1 1.0
O2 A:PO4500 3.8 26.8 1.0
OH A:TYR204 4.0 23.5 0.5
OH A:TYR204 4.0 24.2 0.5
NE2 A:HIS293 4.0 24.6 1.0
ND1 A:HIS210 4.1 22.3 0.5
ND1 A:HIS210 4.1 23.2 0.5
CG A:HIS210 4.2 23.3 0.5
CD2 A:HIS293 4.2 25.1 1.0
CG A:HIS210 4.2 24.0 0.5
CB A:ASP214 4.2 22.8 1.0
O1 A:PO4500 4.2 28.2 1.0
CE1 A:TYR204 4.3 23.9 0.5
CA A:HIS293 4.4 23.7 1.0
CE1 A:TYR204 4.4 24.7 0.5
N A:ASP214 4.5 23.4 1.0
CA A:ASP214 4.6 22.6 1.0
C A:VAL213 4.6 24.4 1.0
CZ A:TYR204 4.6 24.8 0.5
O A:VAL213 4.6 24.2 1.0
CZ A:TYR204 4.6 25.6 0.5
NE2 A:HIS291 4.8 22.9 1.0
O A:HOH705 4.9 26.6 1.0
CD2 A:HIS291 4.9 22.9 1.0
C A:GLY212 5.0 22.4 1.0
O A:GLY212 5.0 23.2 1.0

Zinc binding site 2 out of 2 in 2b44

Go back to Zinc Binding Sites List in 2b44
Zinc binding site 2 out of 2 in the Truncated S. Aureus Lytm, P 32 2 1 Crystal Form


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Truncated S. Aureus Lytm, P 32 2 1 Crystal Form within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn401

b:32.6
occ:1.00
O2 B:PO4600 1.9 31.3 1.0
OD1 B:ASP214 1.9 25.6 1.0
ND1 B:HIS293 2.0 25.6 1.0
NE2 B:HIS210 2.1 26.0 1.0
CG B:ASP214 2.9 24.8 1.0
CE1 B:HIS293 3.0 26.9 1.0
CE1 B:HIS210 3.0 25.8 1.0
P B:PO4600 3.1 31.2 1.0
CG B:HIS293 3.1 24.4 1.0
OD2 B:ASP214 3.1 26.9 1.0
CD2 B:HIS210 3.1 25.3 1.0
O4 B:PO4600 3.2 30.2 1.0
CB B:HIS293 3.5 25.4 1.0
O3 B:PO4600 3.8 32.5 1.0
OH B:TYR204 3.9 28.0 1.0
NE2 B:HIS293 4.1 25.6 1.0
ND1 B:HIS210 4.2 26.2 1.0
CD2 B:HIS293 4.2 27.0 1.0
CB B:ASP214 4.2 24.4 1.0
CG B:HIS210 4.2 27.3 1.0
O1 B:PO4600 4.3 31.4 1.0
CE1 B:TYR204 4.3 27.8 1.0
CA B:HIS293 4.4 24.9 1.0
N B:ASP214 4.4 25.5 1.0
C B:VAL213 4.6 26.7 1.0
CZ B:TYR204 4.6 27.5 1.0
CA B:ASP214 4.6 25.1 1.0
O B:VAL213 4.6 26.3 1.0
NE2 B:HIS291 4.8 24.1 1.0
O B:HOH620 4.9 34.1 1.0
CD2 B:HIS291 5.0 24.6 1.0
C B:GLY212 5.0 27.2 1.0

Reference:

M.Firczuk, A.Mucha, M.Bochtler. Crystal Structures of Active Lytm. J.Mol.Biol. V. 354 578 2005.
ISSN: ISSN 0022-2836
PubMed: 16269153
DOI: 10.1016/J.JMB.2005.09.082
Page generated: Wed Dec 16 03:18:04 2020

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