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Cobalt in PDB 2fqt: Crystal Structure of B.Subtilis Luxs in Complex with (2S)-2-Amino-4- [(2R,3S)-2,3-Dihydroxy-3-N-Hydroxycarbamoyl-Propylmercapto]Butyric Acid

Enzymatic activity of Crystal Structure of B.Subtilis Luxs in Complex with (2S)-2-Amino-4- [(2R,3S)-2,3-Dihydroxy-3-N-Hydroxycarbamoyl-Propylmercapto]Butyric Acid

All present enzymatic activity of Crystal Structure of B.Subtilis Luxs in Complex with (2S)-2-Amino-4- [(2R,3S)-2,3-Dihydroxy-3-N-Hydroxycarbamoyl-Propylmercapto]Butyric Acid:
4.4.1.21;

Protein crystallography data

The structure of Crystal Structure of B.Subtilis Luxs in Complex with (2S)-2-Amino-4- [(2R,3S)-2,3-Dihydroxy-3-N-Hydroxycarbamoyl-Propylmercapto]Butyric Acid, PDB code: 2fqt was solved by G.Shen, R.Rajan, J.Zhu, C.E.Bell, D.Pei, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.38 / 1.79
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 62.860, 62.860, 148.570, 90.00, 90.00, 120.00
R / Rfree (%) 19.4 / 22.6

Cobalt Binding Sites:

The binding sites of Cobalt atom in the Crystal Structure of B.Subtilis Luxs in Complex with (2S)-2-Amino-4- [(2R,3S)-2,3-Dihydroxy-3-N-Hydroxycarbamoyl-Propylmercapto]Butyric Acid (pdb code 2fqt). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total only one binding site of Cobalt was determined in the Crystal Structure of B.Subtilis Luxs in Complex with (2S)-2-Amino-4- [(2R,3S)-2,3-Dihydroxy-3-N-Hydroxycarbamoyl-Propylmercapto]Butyric Acid, PDB code: 2fqt:

Cobalt binding site 1 out of 1 in 2fqt

Go back to Cobalt Binding Sites List in 2fqt
Cobalt binding site 1 out of 1 in the Crystal Structure of B.Subtilis Luxs in Complex with (2S)-2-Amino-4- [(2R,3S)-2,3-Dihydroxy-3-N-Hydroxycarbamoyl-Propylmercapto]Butyric Acid


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Crystal Structure of B.Subtilis Luxs in Complex with (2S)-2-Amino-4- [(2R,3S)-2,3-Dihydroxy-3-N-Hydroxycarbamoyl-Propylmercapto]Butyric Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Co701

b:20.3
occ:1.00
 NE2 A:HIS54 2.1 13.7 1.0
NE2 A:HIS58 2.1 16.8 1.0
O2 A:H1D4398 2.2 22.6 1.0
O3 A:H1D4398 2.3 19.8 1.0
SG A:CYS126 2.3 17.9 1.0
CE1 A:HIS58 2.9 17.2 1.0
CE1 A:HIS54 3.0 14.5 1.0
C2 A:H1D4398 3.0 22.1 1.0
CD2 A:HIS54 3.1 14.4 1.0
CD2 A:HIS58 3.2 17.1 1.0
C3 A:H1D4398 3.2 21.4 1.0
CB A:CYS126 3.6 16.6 1.0
N A:GLY127 3.9 16.7 1.0
C4 A:H1D4398 4.0 21.4 1.0
CA A:CYS126 4.0 17.5 1.0
ND1 A:HIS58 4.1 16.7 1.0
ND1 A:HIS54 4.1 13.9 1.0
CG A:HIS54 4.2 14.8 1.0
NE2 A:HIS132 4.2 17.1 1.0
CG A:HIS58 4.2 16.0 1.0
O A:HOH469 4.3 21.4 1.0
N1 A:H1D4398 4.3 24.4 1.0
CE1 A:HIS132 4.4 16.7 1.0
C A:CYS126 4.4 17.6 1.0
OE1 A:GLU57 4.5 13.9 1.0
C5 A:H1D4398 4.7 21.0 1.0
N A:GLN128 4.8 15.7 1.0
O1 A:H1D4398 4.9 25.0 1.0
CA A:GLY127 4.9 16.6 1.0

Reference:

G.Shen, R.Rajan, J.Zhu, C.E.Bell, D.Pei. Design and Synthesis of Substrate Analogue Inhibitors of S-Ribosylhomocysteinase (Luxs) J.Med.Chem. V. 49 3003 2006.
ISSN: ISSN 0022-2623
PubMed: 16686542
DOI: 10.1021/JM060047G
Page generated: Sun Jul 13 18:14:22 2025

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