Atomistry » Manganese » PDB 2pal-2qgi » 2qb0
Atomistry »
  Manganese »
    PDB 2pal-2qgi »
      2qb0 »

Manganese in PDB 2qb0: Structure of the 2TEL Crystallization Module Fused to T4 Lysozyme with An Ala-Gly-Pro Linker.

Enzymatic activity of Structure of the 2TEL Crystallization Module Fused to T4 Lysozyme with An Ala-Gly-Pro Linker.

All present enzymatic activity of Structure of the 2TEL Crystallization Module Fused to T4 Lysozyme with An Ala-Gly-Pro Linker.:
3.2.1.17;

Protein crystallography data

The structure of Structure of the 2TEL Crystallization Module Fused to T4 Lysozyme with An Ala-Gly-Pro Linker., PDB code: 2qb0 was solved by S.Nauli, J.U.Bowie, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.56
Space group P 32
Cell size a, b, c (Å), α, β, γ (°) 122.620, 122.620, 53.586, 90.00, 90.00, 120.00
R / Rfree (%) 21.1 / 25.2

Manganese Binding Sites:

The binding sites of Manganese atom in the Structure of the 2TEL Crystallization Module Fused to T4 Lysozyme with An Ala-Gly-Pro Linker. (pdb code 2qb0). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 5 binding sites of Manganese where determined in the Structure of the 2TEL Crystallization Module Fused to T4 Lysozyme with An Ala-Gly-Pro Linker., PDB code: 2qb0:
Jump to Manganese binding site number: 1; 2; 3; 4; 5;

Manganese binding site 1 out of 5 in 2qb0

Go back to Manganese Binding Sites List in 2qb0
Manganese binding site 1 out of 5 in the Structure of the 2TEL Crystallization Module Fused to T4 Lysozyme with An Ala-Gly-Pro Linker.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Structure of the 2TEL Crystallization Module Fused to T4 Lysozyme with An Ala-Gly-Pro Linker. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn256

b:0.7
occ:1.00
 OE1 B:GLU104 2.3 57.8 1.0
CD B:GLU104 3.3 52.7 1.0
OE2 B:GLU104 3.7 49.5 1.0
CA B:GLY123 4.1 40.8 1.0
O B:GLY123 4.4 54.4 1.0
CG B:GLU104 4.7 53.3 1.0
NH1 B:ARG238 4.7 50.4 1.0
C B:GLY123 4.7 44.4 1.0
CB B:GLU104 4.9 51.7 1.0

Manganese binding site 2 out of 5 in 2qb0

Go back to Manganese Binding Sites List in 2qb0
Manganese binding site 2 out of 5 in the Structure of the 2TEL Crystallization Module Fused to T4 Lysozyme with An Ala-Gly-Pro Linker.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Structure of the 2TEL Crystallization Module Fused to T4 Lysozyme with An Ala-Gly-Pro Linker. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn257

b:49.0
occ:1.00
 O B:HOH277 2.2 40.2 1.0
O B:HOH286 2.2 44.0 1.0
OD1 B:ASP154 2.3 48.5 1.0
ND1 B:HIS21 2.3 41.0 1.0
OD1 B:ASP33 2.4 53.6 1.0
OE1 B:GLU157 2.4 55.6 1.0
CE1 B:HIS21 3.0 34.3 1.0
CG B:ASP33 3.1 55.6 1.0
CG B:ASP154 3.3 52.5 1.0
OD2 B:ASP33 3.3 43.0 1.0
CG B:HIS21 3.4 37.6 1.0
CD B:GLU157 3.4 54.9 1.0
OE2 B:GLU157 3.7 58.3 1.0
OD2 B:ASP154 3.8 52.1 1.0
CB B:HIS21 3.8 36.0 1.0
O B:HIS21 3.9 43.0 1.0
NE2 B:HIS21 4.2 46.1 1.0
O B:HOH281 4.2 46.5 1.0
CA B:ASP154 4.3 62.7 1.0
CD2 B:HIS21 4.4 42.2 1.0
CB B:ASP154 4.4 49.6 1.0
C B:HIS21 4.4 49.1 1.0
CB B:ASP33 4.5 54.7 1.0
N B:ASP154 4.6 69.7 1.0
CA B:HIS21 4.7 45.2 1.0
CG B:GLU157 4.7 50.4 1.0
CD2 B:LEU22 4.9 47.9 1.0
NE2 B:GLN36 4.9 57.6 1.0

Manganese binding site 3 out of 5 in 2qb0

Go back to Manganese Binding Sites List in 2qb0
Manganese binding site 3 out of 5 in the Structure of the 2TEL Crystallization Module Fused to T4 Lysozyme with An Ala-Gly-Pro Linker.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Structure of the 2TEL Crystallization Module Fused to T4 Lysozyme with An Ala-Gly-Pro Linker. within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mn207

b:92.3
occ:1.00
 OG C:SER74 3.0 44.1 1.0
O C:HOH212 3.1 39.3 1.0
N C:HIS76 3.6 48.7 1.0
CA C:SER74 3.7 37.8 1.0
CB C:SER74 3.7 36.5 1.0
CB C:HIS76 3.8 40.8 1.0
ND1 C:HIS76 3.8 44.7 1.0
C C:SER74 3.9 39.2 1.0
N C:PRO75 4.0 37.3 1.0
CD C:PRO75 4.0 39.9 1.0
CD1 C:ILE50 4.1 63.8 1.0
CA C:HIS76 4.2 44.0 1.0
N C:SER77 4.2 41.5 1.0
CG C:HIS76 4.2 46.5 1.0
O C:SER74 4.5 42.0 1.0
C C:HIS76 4.6 46.9 1.0
C C:PRO75 4.7 43.8 1.0
O C:PRO49 4.7 49.1 1.0
CA C:PRO75 4.8 41.9 1.0
CB C:SER77 4.9 45.2 1.0
OG C:SER77 4.9 56.0 1.0

Manganese binding site 4 out of 5 in 2qb0

Go back to Manganese Binding Sites List in 2qb0
Manganese binding site 4 out of 5 in the Structure of the 2TEL Crystallization Module Fused to T4 Lysozyme with An Ala-Gly-Pro Linker.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Structure of the 2TEL Crystallization Module Fused to T4 Lysozyme with An Ala-Gly-Pro Linker. within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mn256

b:0.1
occ:1.00
 OE1 D:GLU104 2.3 57.8 1.0
CD D:GLU104 3.3 52.7 1.0
OE2 D:GLU104 3.7 49.6 1.0
CA D:GLY123 4.2 40.9 1.0
O D:GLY123 4.5 54.3 1.0
NH1 D:ARG238 4.7 50.4 1.0
CG D:GLU104 4.7 53.3 1.0
C D:GLY123 4.8 44.4 1.0
CB D:GLU104 4.9 51.8 1.0

Manganese binding site 5 out of 5 in 2qb0

Go back to Manganese Binding Sites List in 2qb0
Manganese binding site 5 out of 5 in the Structure of the 2TEL Crystallization Module Fused to T4 Lysozyme with An Ala-Gly-Pro Linker.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 5 of Structure of the 2TEL Crystallization Module Fused to T4 Lysozyme with An Ala-Gly-Pro Linker. within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mn257

b:0.1
occ:1.00
 OD1 D:ASP154 2.5 48.5 1.0
OE1 D:GLU157 2.5 55.7 1.0
OD2 D:ASP33 2.7 42.9 1.0
OD1 D:ASP33 2.7 53.6 1.0
O D:HOH276 2.8 44.7 1.0
OE2 D:GLU157 2.8 58.3 1.0
CG D:ASP33 3.0 55.6 1.0
CD D:GLU157 3.0 54.9 1.0
CG D:ASP154 3.7 52.5 1.0
ND1 D:HIS21 3.8 40.9 1.0
OD2 D:ASP154 4.3 52.1 1.0
CE1 D:HIS21 4.4 34.4 1.0
CB D:ASP33 4.5 54.7 1.0
CG D:GLU157 4.5 50.4 1.0
CA D:ASP154 4.6 62.8 1.0
OG D:SER30 4.6 34.5 1.0
O D:HOH288 4.6 52.1 1.0
CB D:ASP154 4.7 49.5 1.0
O D:HIS21 4.8 42.9 1.0
N D:ASP154 4.8 69.7 1.0
CG D:HIS21 4.8 37.6 1.0

Reference:

S.Nauli, S.Farr, Y.J.Lee, H.Y.Kim, S.Faham, J.U.Bowie. Polymer-Driven Crystallization. Protein Sci. V. 16 2542 2007.
ISSN: ISSN 0961-8368
PubMed: 17962407
DOI: 10.1110/PS.073074207
Page generated: Sat Oct 5 14:59:29 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy