Zinc in PDB 5i1t: 2.6 Angstrom Resolution Crystal Structure of Stage II Sporulation Protein D (Spoiid) From Clostridium Difficile in Complex with Triacetylchitotriose

Protein crystallography data

The structure of 2.6 Angstrom Resolution Crystal Structure of Stage II Sporulation Protein D (Spoiid) From Clostridium Difficile in Complex with Triacetylchitotriose, PDB code: 5i1t was solved by S.Nocadello, G.Minasov, L.Shuvalova, I.Dubrovska, S.Grimshaw, K.Kwon, W.F.Anderson, 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) 29.08 / 2.60
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 98.082, 98.082, 108.327, 90.00, 90.00, 120.00
R / Rfree (%) 15.5 / 19.6

Other elements in 5i1t:

The structure of 2.6 Angstrom Resolution Crystal Structure of Stage II Sporulation Protein D (Spoiid) From Clostridium Difficile in Complex with Triacetylchitotriose also contains other interesting chemical elements:

Chlorine (Cl) 1 atom
Sodium (Na) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the 2.6 Angstrom Resolution Crystal Structure of Stage II Sporulation Protein D (Spoiid) From Clostridium Difficile in Complex with Triacetylchitotriose (pdb code 5i1t). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the 2.6 Angstrom Resolution Crystal Structure of Stage II Sporulation Protein D (Spoiid) From Clostridium Difficile in Complex with Triacetylchitotriose, PDB code: 5i1t:

Zinc binding site 1 out of 1 in 5i1t

Go back to Zinc Binding Sites List in 5i1t
Zinc binding site 1 out of 1 in the 2.6 Angstrom Resolution Crystal Structure of Stage II Sporulation Protein D (Spoiid) From Clostridium Difficile in Complex with Triacetylchitotriose


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of 2.6 Angstrom Resolution Crystal Structure of Stage II Sporulation Protein D (Spoiid) From Clostridium Difficile in Complex with Triacetylchitotriose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:75.0
occ:1.00
ND1 A:HIS145 2.1 90.3 1.0
NE2 A:HIS134 2.2 91.5 1.0
SG A:CYS140 2.3 80.5 1.0
SG A:CYS146 2.3 78.3 1.0
CE1 A:HIS145 3.1 92.3 1.0
CE1 A:HIS134 3.1 87.5 1.0
CG A:HIS145 3.2 88.8 1.0
CD2 A:HIS134 3.2 89.8 1.0
CB A:CYS146 3.4 74.8 1.0
CB A:CYS140 3.4 80.3 1.0
N A:CYS140 3.5 72.5 1.0
CB A:HIS145 3.5 81.0 1.0
N A:CYS146 3.6 72.5 1.0
C A:HIS145 3.9 76.7 1.0
CA A:CYS140 3.9 75.6 1.0
CA A:CYS146 4.0 71.8 1.0
NE2 A:HIS145 4.2 92.1 1.0
ND1 A:HIS134 4.3 90.5 1.0
CD2 A:HIS145 4.3 91.0 1.0
CG A:HIS134 4.3 92.7 1.0
C A:VAL139 4.3 75.2 1.0
CA A:HIS145 4.4 77.2 1.0
O A:HIS145 4.4 69.3 1.0
O A:CYS140 4.6 66.5 1.0
C A:CYS140 4.6 71.1 1.0
CA A:VAL139 4.6 76.2 1.0

Reference:

S.Nocadello, G.Minasov, L.S.Shuvalova, I.Dubrovska, E.Sabini, W.F.Anderson. Crystal Structures of the Spoiid Lytic Transglycosylases Essential For Bacterial Sporulation. J.Biol.Chem. V. 291 14915 2016.
ISSN: ESSN 1083-351X
PubMed: 27226615
DOI: 10.1074/JBC.M116.729749
Page generated: Wed Dec 16 06:21:13 2020

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