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Chlorine in PDB 2b3h: Crystal Structure of Human Methionine Aminopeptidase Type I with A Third Cobalt in the Active Site

Enzymatic activity of Crystal Structure of Human Methionine Aminopeptidase Type I with A Third Cobalt in the Active Site

All present enzymatic activity of Crystal Structure of Human Methionine Aminopeptidase Type I with A Third Cobalt in the Active Site:
3.4.11.18;

Protein crystallography data

The structure of Crystal Structure of Human Methionine Aminopeptidase Type I with A Third Cobalt in the Active Site, PDB code: 2b3h was solved by A.Addlagatta, X.Hu, J.O.Liu, B.W.Matthews, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.10
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 47.290, 77.300, 48.340, 90.00, 91.03, 90.00
R / Rfree (%) 9.8 / 13.1

Other elements in 2b3h:

The structure of Crystal Structure of Human Methionine Aminopeptidase Type I with A Third Cobalt in the Active Site also contains other interesting chemical elements:

Cobalt (Co) 4 atoms
Potassium (K) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Human Methionine Aminopeptidase Type I with A Third Cobalt in the Active Site (pdb code 2b3h). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of Human Methionine Aminopeptidase Type I with A Third Cobalt in the Active Site, PDB code: 2b3h:

Chlorine binding site 1 out of 1 in 2b3h

Go back to Chlorine Binding Sites List in 2b3h
Chlorine binding site 1 out of 1 in the Crystal Structure of Human Methionine Aminopeptidase Type I with A Third Cobalt in the Active Site


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Human Methionine Aminopeptidase Type I with A Third Cobalt in the Active Site within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl406

b:46.3
occ:0.50
 O A:HOH937 0.7 8.5 0.4
O A:HOH510 2.1 9.1 1.0
CO A:CO403 2.3 10.7 0.5
O3 A:GOL471 2.7 38.3 1.0
O A:HOH933 2.9 20.7 0.4
O A:HOH935 2.9 19.6 0.5
O A:HOH934 2.9 19.1 0.5
O A:HOH505 3.0 10.0 1.0
CO A:CO404 3.0 16.7 0.2
NE2 A:HIS310 3.1 12.6 1.0
O A:HOH936 3.1 13.9 0.5
O1 A:GOL471 3.3 23.1 1.0
CO A:CO401 3.3 8.8 1.0
CO A:CO402 3.6 7.7 1.0
NE2 A:HIS303 3.9 8.2 1.0
OD2 A:ASP240 3.9 8.1 1.0
CE1 A:HIS310 4.0 13.6 1.0
C3 A:GOL471 4.0 27.2 1.0
CD2 A:HIS310 4.0 13.9 1.0
OE2 A:GLU336 4.1 13.7 1.0
OD2 A:ASP229 4.1 14.5 1.0
CE1 A:PHE309 4.2 10.8 1.0
O A:HOH939 4.2 21.7 0.4
CZ A:PHE309 4.4 10.3 1.0
NE2 A:HIS212 4.4 14.2 1.0
OE1 A:GLU336 4.4 9.2 1.0
CD2 A:HIS303 4.6 9.0 1.0
C1 A:GOL471 4.6 27.5 1.0
CE1 A:HIS303 4.6 8.8 1.0
OD1 A:ASP240 4.7 7.7 1.0
CG A:ASP240 4.7 7.9 1.0
CD A:GLU336 4.7 9.3 1.0
C2 A:GOL471 4.7 20.5 1.0
O A:HOH938 4.9 53.0 1.0
O A:HOH688 5.0 16.7 1.0

Reference:

A.Addlagatta, X.Hu, J.O.Liu, B.W.Matthews. Structural Basis For the Functional Differences Between Type I and Type II Human Methionine Aminopeptidases(,). Biochemistry V. 44 14741 2005.
ISSN: ISSN 0006-2960
PubMed: 16274222
DOI: 10.1021/BI051691K
Page generated: Sat Jul 20 05:31:17 2024

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