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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

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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

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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: Tue Dec 15 04:04:51 2020

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