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Chlorine in PDB 6dvv: 2.25 Angstrom Resolution Crystal Structure of 6-Phospho-Alpha- Glucosidase From Klebsiella Pneumoniae in Complex with Nad and MN2+.

Enzymatic activity of 2.25 Angstrom Resolution Crystal Structure of 6-Phospho-Alpha- Glucosidase From Klebsiella Pneumoniae in Complex with Nad and MN2+.

All present enzymatic activity of 2.25 Angstrom Resolution Crystal Structure of 6-Phospho-Alpha- Glucosidase From Klebsiella Pneumoniae in Complex with Nad and MN2+.:
3.2.1.122;

Protein crystallography data

The structure of 2.25 Angstrom Resolution Crystal Structure of 6-Phospho-Alpha- Glucosidase From Klebsiella Pneumoniae in Complex with Nad and MN2+., PDB code: 6dvv was solved by G.Minasov, L.Shuvalova, O.Kiryukhina, M.Endres, K.J.F.Satchell, A.Joachimiak, Center For Structural Genomics Of Infectious Diseases(Csgid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.99 / 2.25
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 86.027, 86.027, 230.777, 90.00, 90.00, 120.00
R / Rfree (%) 16.4 / 21.9

Other elements in 6dvv:

The structure of 2.25 Angstrom Resolution Crystal Structure of 6-Phospho-Alpha- Glucosidase From Klebsiella Pneumoniae in Complex with Nad and MN2+. also contains other interesting chemical elements:

Manganese (Mn) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the 2.25 Angstrom Resolution Crystal Structure of 6-Phospho-Alpha- Glucosidase From Klebsiella Pneumoniae in Complex with Nad and MN2+. (pdb code 6dvv). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the 2.25 Angstrom Resolution Crystal Structure of 6-Phospho-Alpha- Glucosidase From Klebsiella Pneumoniae in Complex with Nad and MN2+., PDB code: 6dvv:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 6dvv

Go back to Chlorine Binding Sites List in 6dvv
Chlorine binding site 1 out of 2 in the 2.25 Angstrom Resolution Crystal Structure of 6-Phospho-Alpha- Glucosidase From Klebsiella Pneumoniae in Complex with Nad and MN2+.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of 2.25 Angstrom Resolution Crystal Structure of 6-Phospho-Alpha- Glucosidase From Klebsiella Pneumoniae in Complex with Nad and MN2+. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl502

b:94.7
occ:1.00
O B:HOH633 3.1 59.4 1.0
OD1 B:ASP351 3.1 53.4 1.0
NZ B:LYS380 3.3 51.9 1.0
O B:HOH759 3.4 48.4 1.0
N B:ASP351 3.5 39.0 1.0
CG B:ASP351 3.6 47.6 1.0
CA B:PHE350 3.7 35.1 1.0
CD1 B:PHE350 3.8 39.7 1.0
OD2 B:ASP351 3.8 59.4 1.0
O B:ASN349 4.0 38.3 1.0
OG B:SER384 4.0 35.5 1.0
C B:PHE350 4.0 38.1 1.0
CG B:PHE350 4.3 36.7 1.0
CE1 B:PHE350 4.4 41.1 1.0
CA B:ASP351 4.4 39.1 1.0
CB B:PHE350 4.5 36.8 1.0
CB B:ASP351 4.5 44.5 1.0
N B:PHE350 4.6 35.2 1.0
C B:ASN349 4.6 35.8 1.0
CE B:LYS380 4.7 47.3 1.0

Chlorine binding site 2 out of 2 in 6dvv

Go back to Chlorine Binding Sites List in 6dvv
Chlorine binding site 2 out of 2 in the 2.25 Angstrom Resolution Crystal Structure of 6-Phospho-Alpha- Glucosidase From Klebsiella Pneumoniae in Complex with Nad and MN2+.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of 2.25 Angstrom Resolution Crystal Structure of 6-Phospho-Alpha- Glucosidase From Klebsiella Pneumoniae in Complex with Nad and MN2+. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl503

b:82.7
occ:1.00
O4 B:SO4506 3.1 59.9 0.5
O3 B:SO4506 3.8 44.7 0.5
S B:SO4506 3.9 57.0 0.5
CB B:PRO376 4.1 38.0 1.0
O1 B:SO4506 4.3 63.1 0.5
CG B:PRO376 4.3 39.1 1.0
CA B:PRO376 4.9 38.0 1.0

Reference:

G.Minasov, L.Shuvalova, O.Kiryukhina, M.Endres, K.J.F.Satchell, A.Joachimiak, Center For Structural Genomics Of Infectious Diseases(Csgid). 2.25 Angstrom Resolution Crystal Structure of 6-Phospho-Alpha-Glucosidase From Klebsiella Pneumoniae in Complex with Nad and MN2+. To Be Published.
Page generated: Sat Jul 12 13:03:06 2025

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