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Sodium in PDB 2evm: Crystal Structure of Methionine Aminopeptidase in Complex with 5-(2,5-Dichlorophenyl)Furan-2-Carboxylic Acid

Enzymatic activity of Crystal Structure of Methionine Aminopeptidase in Complex with 5-(2,5-Dichlorophenyl)Furan-2-Carboxylic Acid

All present enzymatic activity of Crystal Structure of Methionine Aminopeptidase in Complex with 5-(2,5-Dichlorophenyl)Furan-2-Carboxylic Acid:
3.4.11.18;

Protein crystallography data

The structure of Crystal Structure of Methionine Aminopeptidase in Complex with 5-(2,5-Dichlorophenyl)Furan-2-Carboxylic Acid, PDB code: 2evm was solved by W.-J.Huang, 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 (°) 37.800, 60.200, 50.400, 90.00, 104.50, 90.00
R / Rfree (%) 21.5 / 24.8

Other elements in 2evm:

The structure of Crystal Structure of Methionine Aminopeptidase in Complex with 5-(2,5-Dichlorophenyl)Furan-2-Carboxylic Acid also contains other interesting chemical elements:

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

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of Methionine Aminopeptidase in Complex with 5-(2,5-Dichlorophenyl)Furan-2-Carboxylic Acid (pdb code 2evm). 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 Crystal Structure of Methionine Aminopeptidase in Complex with 5-(2,5-Dichlorophenyl)Furan-2-Carboxylic Acid, PDB code: 2evm:

Sodium binding site 1 out of 1 in 2evm

Go back to Sodium Binding Sites List in 2evm
Sodium binding site 1 out of 1 in the Crystal Structure of Methionine Aminopeptidase in Complex with 5-(2,5-Dichlorophenyl)Furan-2-Carboxylic Acid


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of Methionine Aminopeptidase in Complex with 5-(2,5-Dichlorophenyl)Furan-2-Carboxylic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na903

b:13.5
occ:1.00
 O A:ASN74 2.2 13.0 1.0
O A:SER231 2.2 12.6 1.0
O A:VAL76 2.3 9.9 1.0
O A:HOH1006 2.3 11.9 1.0
C A:ASN74 3.2 12.3 1.0
C A:SER231 3.3 10.7 1.0
C A:VAL76 3.4 10.6 1.0
N A:ASN74 3.6 10.5 1.0
CA A:ASN74 3.7 11.4 1.0
N A:SER231 3.8 11.7 1.0
CB A:SER231 3.8 11.1 1.0
CA A:SER231 3.8 11.7 1.0
O A:HOH1001 3.8 8.9 1.0
N A:VAL76 3.9 12.3 1.0
C A:ILE73 3.9 10.3 1.0
O A:ILE73 4.1 9.8 1.0
N A:GLU75 4.2 13.9 1.0
CA A:VAL76 4.2 11.7 1.0
C A:GLU75 4.2 13.4 1.0
O A:SER72 4.3 10.0 1.0
N A:VAL77 4.3 9.9 1.0
N A:ALA232 4.4 9.6 1.0
O A:HOH1011 4.4 12.5 1.0
CA A:VAL77 4.5 10.7 1.0
CD1 A:ILE93 4.5 17.3 1.0
OG A:SER231 4.5 11.3 1.0
C A:SER72 4.6 11.2 1.0
CA A:GLU75 4.6 13.6 1.0
CA A:ILE73 4.6 10.1 1.0
N A:ILE73 4.7 10.3 1.0
CA A:ALA232 4.7 9.8 1.0
CB A:SER72 4.7 10.5 1.0
CG1 A:ILE93 4.8 13.6 1.0
CB A:VAL76 4.8 11.4 1.0
CE A:MET112 4.8 8.0 1.0
O A:GLU75 4.9 13.8 1.0
O A:VAL77 4.9 10.6 1.0
C A:VAL77 5.0 11.2 1.0
O A:ILE93 5.0 8.7 1.0

Reference:

S.X.Xie, W.J.Huang, Z.Q.Ma, M.Huang, R.P.Hanzlik, Q.Z.Ye. Structural Analysis of Metalloform-Selective Inhibition of Methionine Aminopeptidase. Acta Crystallogr.,Sect.D V. 62 425 2006.
ISSN: ISSN 0907-4449
PubMed: 16552144
DOI: 10.1107/S0907444906003878
Page generated: Sun Aug 17 10:28:25 2025

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