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Sodium in PDB 2gu5: E. Coli Methionine Aminopeptidase in Complex with Nlep, 1: 1, Di-Metalated

Enzymatic activity of E. Coli Methionine Aminopeptidase in Complex with Nlep, 1: 1, Di-Metalated

All present enzymatic activity of E. Coli Methionine Aminopeptidase in Complex with Nlep, 1: 1, Di-Metalated:
3.4.11.18;

Protein crystallography data

The structure of E. Coli Methionine Aminopeptidase in Complex with Nlep, 1: 1, Di-Metalated, PDB code: 2gu5 was solved by Q.Z.Ye, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 14.19 / 1.60
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 49.790, 64.606, 76.354, 90.00, 107.77, 90.00
R / Rfree (%) 21.1 / 23.3

Other elements in 2gu5:

The structure of E. Coli Methionine Aminopeptidase in Complex with Nlep, 1: 1, Di-Metalated also contains other interesting chemical elements:

Manganese (Mn) 4 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the E. Coli Methionine Aminopeptidase in Complex with Nlep, 1: 1, Di-Metalated (pdb code 2gu5). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the E. Coli Methionine Aminopeptidase in Complex with Nlep, 1: 1, Di-Metalated, PDB code: 2gu5:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in 2gu5

Go back to Sodium Binding Sites List in 2gu5
Sodium binding site 1 out of 2 in the E. Coli Methionine Aminopeptidase in Complex with Nlep, 1: 1, Di-Metalated


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of E. Coli Methionine Aminopeptidase in Complex with Nlep, 1: 1, Di-Metalated within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na300

b:8.2
occ:1.00
O A:ASN74 2.2 8.3 1.0
O A:SER231 2.3 6.8 1.0
O A:HOH3829 2.3 10.5 1.0
O A:VAL76 2.3 11.7 1.0
C A:ASN74 3.2 8.3 1.0
C A:SER231 3.3 7.4 1.0
O A:HOH3809 3.4 8.3 1.0
C A:VAL76 3.5 9.5 1.0
N A:ASN74 3.6 9.7 1.0
CA A:ASN74 3.8 9.5 1.0
N A:SER231 3.8 8.1 1.0
CB A:SER231 3.9 8.4 1.0
CA A:SER231 3.9 8.5 1.0
N A:VAL76 3.9 8.2 1.0
C A:ILE73 3.9 9.4 1.0
O A:ILE73 4.2 7.9 1.0
CA A:VAL76 4.3 8.7 1.0
N A:GLU75 4.3 9.5 1.0
C A:GLU75 4.3 9.9 1.0
O A:HOH3810 4.4 7.3 1.0
O A:SER72 4.4 8.0 1.0
N A:ALA232 4.4 7.1 1.0
CD1 A:ILE93 4.4 12.2 1.0
N A:VAL77 4.4 8.9 1.0
CG1 A:ILE93 4.6 7.8 1.0
C A:SER72 4.6 7.9 1.0
CA A:VAL77 4.6 8.3 1.0
CA A:ILE73 4.6 9.4 1.0
OG A:SER231 4.6 8.5 1.0
CA A:GLU75 4.7 10.1 1.0
N A:ILE73 4.7 9.2 1.0
CA A:ALA232 4.7 7.2 1.0
CB A:VAL76 4.7 8.9 1.0
CB A:SER72 4.8 8.0 1.0
O A:ILE93 4.9 9.2 1.0
CE A:MET112 4.9 7.8 1.0
O A:GLU75 5.0 9.5 1.0

Sodium binding site 2 out of 2 in 2gu5

Go back to Sodium Binding Sites List in 2gu5
Sodium binding site 2 out of 2 in the E. Coli Methionine Aminopeptidase in Complex with Nlep, 1: 1, Di-Metalated


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of E. Coli Methionine Aminopeptidase in Complex with Nlep, 1: 1, Di-Metalated within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Na300

b:9.4
occ:1.00
O B:HOH3817 2.2 11.6 1.0
O B:ASN74 2.2 9.5 1.0
O B:SER231 2.3 7.9 1.0
O B:VAL76 2.3 10.7 1.0
C B:ASN74 3.2 10.4 1.0
C B:SER231 3.3 8.0 1.0
O B:HOH3809 3.4 9.9 1.0
C B:VAL76 3.5 10.4 1.0
N B:ASN74 3.7 10.0 1.0
CA B:ASN74 3.8 10.8 1.0
N B:SER231 3.8 7.5 1.0
CB B:SER231 3.9 7.6 1.0
CA B:SER231 3.9 7.9 1.0
N B:VAL76 3.9 9.2 1.0
C B:ILE73 3.9 10.4 1.0
O B:ILE73 4.2 9.3 1.0
CA B:VAL76 4.2 8.8 1.0
N B:GLU75 4.3 11.7 1.0
C B:GLU75 4.3 10.2 1.0
O B:HOH3810 4.4 8.6 1.0
CD1 B:ILE93 4.4 10.5 1.0
N B:ALA232 4.4 8.4 1.0
O B:SER72 4.4 8.4 1.0
N B:VAL77 4.5 9.4 1.0
CG1 B:ILE93 4.6 8.2 1.0
CA B:GLU75 4.6 11.5 1.0
C B:SER72 4.6 8.8 1.0
CA B:VAL77 4.6 10.7 1.0
CA B:ILE73 4.6 9.5 1.0
OG B:SER231 4.7 8.9 1.0
N B:ILE73 4.7 8.3 1.0
CB B:VAL76 4.7 8.6 1.0
CA B:ALA232 4.7 8.4 1.0
CB B:SER72 4.7 8.6 1.0
O B:GLU75 4.9 9.2 1.0
CE B:MET112 4.9 9.3 1.0
O B:ILE93 4.9 10.9 1.0

Reference:

Q.Z.Ye, S.X.Xie, Z.Q.Ma, M.Huang, R.P.Hanzlik. Structural Basis of Catalysis By Monometalated Methionine Aminopeptidase. Proc.Natl.Acad.Sci.Usa V. 103 9470 2006.
ISSN: ISSN 0027-8424
PubMed: 16769889
DOI: 10.1073/PNAS.0602433103
Page generated: Mon Oct 7 02:41:43 2024

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