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Chlorine in PDB 6xdk: Crystal Structure of Phosphoserine Aminotransferase (Serc) From Stenotrophomonas Maltophilia K279A

Enzymatic activity of Crystal Structure of Phosphoserine Aminotransferase (Serc) From Stenotrophomonas Maltophilia K279A

All present enzymatic activity of Crystal Structure of Phosphoserine Aminotransferase (Serc) From Stenotrophomonas Maltophilia K279A:
2.6.1.52;

Protein crystallography data

The structure of Crystal Structure of Phosphoserine Aminotransferase (Serc) From Stenotrophomonas Maltophilia K279A, PDB code: 6xdk was solved by Seattle Structural Genomics Center For Infectious Disease (Ssgcid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.85 / 1.60
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 64.350, 71.620, 89.860, 84.99, 88.82, 63.37
R / Rfree (%) 15.6 / 18.1

Other elements in 6xdk:

The structure of Crystal Structure of Phosphoserine Aminotransferase (Serc) From Stenotrophomonas Maltophilia K279A also contains other interesting chemical elements:

Calcium (Ca) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Phosphoserine Aminotransferase (Serc) From Stenotrophomonas Maltophilia K279A (pdb code 6xdk). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of Phosphoserine Aminotransferase (Serc) From Stenotrophomonas Maltophilia K279A, PDB code: 6xdk:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 6xdk

Go back to Chlorine Binding Sites List in 6xdk
Chlorine binding site 1 out of 2 in the Crystal Structure of Phosphoserine Aminotransferase (Serc) From Stenotrophomonas Maltophilia K279A


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 Phosphoserine Aminotransferase (Serc) From Stenotrophomonas Maltophilia K279A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl400

b:21.7
occ:1.00
O B:HOH898 2.9 35.1 1.0
NE2 A:GLN195 3.0 30.1 1.0
O B:HOH695 3.1 21.9 1.0
N A:GLY202 3.2 17.7 1.0
CA A:GLY202 3.4 18.4 1.0
O A:HOH670 3.5 20.9 1.0
C A:PRO200 3.5 18.5 1.0
CA A:PRO200 3.6 17.0 1.0
CG A:GLN195 3.8 21.2 1.0
N A:VAL201 3.8 17.9 1.0
CD A:GLN195 3.9 31.6 1.0
O A:PRO200 3.9 19.1 1.0
CB A:PRO200 3.9 17.8 1.0
CB B:PRO240 4.0 17.6 1.0
CB A:ALA194 4.1 19.1 1.0
C A:VAL201 4.2 21.1 1.0
CG B:PRO240 4.3 19.5 1.0
CA B:PRO240 4.5 17.7 1.0
O B:HOH753 4.5 20.5 1.0
CA A:VAL201 4.6 15.8 1.0
C A:GLY202 4.8 21.4 1.0
O B:HOH568 4.8 16.6 1.0
O B:HOH628 4.8 38.5 1.0
N A:GLN195 4.9 17.4 1.0
N A:PRO200 5.0 18.9 1.0

Chlorine binding site 2 out of 2 in 6xdk

Go back to Chlorine Binding Sites List in 6xdk
Chlorine binding site 2 out of 2 in the Crystal Structure of Phosphoserine Aminotransferase (Serc) From Stenotrophomonas Maltophilia K279A


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Phosphoserine Aminotransferase (Serc) From Stenotrophomonas Maltophilia K279A within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cl400

b:19.9
occ:1.00
O D:HOH856 3.0 35.7 1.0
NE2 D:GLN195 3.1 19.2 0.6
O C:HOH683 3.1 23.2 1.0
N D:GLY202 3.2 17.2 1.0
O D:HOH620 3.4 22.1 1.0
CA D:GLY202 3.4 19.5 1.0
C D:PRO200 3.6 16.6 1.0
CA D:PRO200 3.6 17.1 1.0
CG D:GLN195 3.7 21.5 0.4
NE2 D:GLN195 3.8 23.4 0.4
N D:VAL201 3.8 19.7 1.0
O D:PRO200 4.0 18.1 1.0
CG D:GLN195 4.0 21.4 0.6
CB C:PRO240 4.0 20.4 1.0
CD D:GLN195 4.0 23.0 0.6
CB D:PRO200 4.1 16.9 1.0
CB D:ALA194 4.1 19.9 1.0
C D:VAL201 4.1 20.1 1.0
CG C:PRO240 4.3 20.9 1.0
CD D:GLN195 4.3 23.7 0.4
CA C:PRO240 4.5 20.4 1.0
CA D:VAL201 4.6 17.5 1.0
O C:HOH740 4.6 21.2 1.0
O C:HOH637 4.8 18.2 1.0
C D:GLY202 4.8 21.7 1.0
N D:GLN195 4.9 17.8 1.0
N D:PRO200 5.0 17.3 1.0

Reference:

J.Abendroth, P.S.Horanyi, D.D.Lorimer, T.E.Edwards. Crystal Structure of Phosphoserine Aminotransferase (Serc) From Stenotrophomonas Maltophilia K279A To Be Published.
Page generated: Sat Jul 12 21:37:24 2025

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