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Sodium in PDB 2q95: E. Coli Methionine Aminopeptidase Mn-Form with Inhibitor A05

Enzymatic activity of E. Coli Methionine Aminopeptidase Mn-Form with Inhibitor A05

All present enzymatic activity of E. Coli Methionine Aminopeptidase Mn-Form with Inhibitor A05:
3.4.11.18;

Protein crystallography data

The structure of E. Coli Methionine Aminopeptidase Mn-Form with Inhibitor A05, PDB code: 2q95 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) 20.00 / 1.70
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 38.847, 62.373, 52.422, 90.00, 108.39, 90.00
R / Rfree (%) 21.4 / 23.9

Other elements in 2q95:

The structure of E. Coli Methionine Aminopeptidase Mn-Form with Inhibitor A05 also contains other interesting chemical elements:

Manganese (Mn) 2 atoms
Chlorine (Cl) 1 atom

Sodium Binding Sites:

The binding sites of Sodium atom in the E. Coli Methionine Aminopeptidase Mn-Form with Inhibitor A05 (pdb code 2q95). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the E. Coli Methionine Aminopeptidase Mn-Form with Inhibitor A05, PDB code: 2q95:

Sodium binding site 1 out of 1 in 2q95

Go back to Sodium Binding Sites List in 2q95
Sodium binding site 1 out of 1 in the E. Coli Methionine Aminopeptidase Mn-Form with Inhibitor A05


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 Mn-Form with Inhibitor A05 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na500

b:16.3
occ:1.00
O A:SER231 2.4 12.5 1.0
O A:ASN74 2.4 17.3 1.0
O A:VAL76 2.5 17.0 1.0
O A:HOH537 2.5 16.6 1.0
C A:ASN74 3.3 17.4 1.0
C A:SER231 3.4 13.3 1.0
C A:VAL76 3.5 16.1 1.0
N A:ASN74 3.6 14.8 1.0
O A:HOH502 3.7 15.8 1.0
CA A:ASN74 3.7 16.7 1.0
C A:ILE73 3.8 14.0 1.0
N A:SER231 3.9 15.1 1.0
N A:VAL76 4.0 16.9 1.0
O A:ILE73 4.0 14.1 1.0
CB A:SER231 4.0 15.2 1.0
CA A:SER231 4.0 14.5 1.0
O A:SER72 4.3 14.1 1.0
CA A:VAL76 4.3 16.4 1.0
N A:GLU75 4.3 17.8 1.0
C A:GLU75 4.4 18.2 1.0
C A:SER72 4.4 15.0 1.0
CA A:ILE73 4.5 14.0 1.0
N A:VAL77 4.5 16.1 1.0
O A:HOH510 4.5 16.9 1.0
N A:ILE73 4.5 14.4 1.0
N A:ALA232 4.5 13.3 1.0
CD1 A:ILE93 4.6 19.9 1.0
CB A:SER72 4.6 14.9 1.0
CA A:VAL77 4.7 15.2 1.0
CA A:GLU75 4.7 18.1 1.0
CG1 A:ILE93 4.7 18.3 1.0
CB A:VAL76 4.8 16.7 1.0
CA A:ALA232 4.8 13.2 1.0
CE A:MET112 4.8 12.5 1.0
OG A:SER231 4.8 15.6 1.0
O A:ILE93 4.8 14.6 1.0
O A:GLU75 4.9 18.6 1.0

Reference:

Z.Q.Ma, S.X.Xie, Q.Q.Huang, F.J.Nan, T.D.Hurley, Q.Z.Ye. Structural Analysis of Inhibition of E. Coli Methionine Aminopeptidase: Implication of Loop Flexibility in Selective Inhibition of Bacterial Enzymes. Bmc Struct.Biol. V. 7 84 2007.
ISSN: ESSN 1472-6807
PubMed: 18093325
DOI: 10.1186/1472-6807-7-84
Page generated: Thu Oct 29 04:15:05 2020

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