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Chlorine in PDB 1zro: Crystal Structure of Eba-175 Region II (Rii) Crystallized in the Presence of (Alpha)2,3-Sialyllactose

Protein crystallography data

The structure of Crystal Structure of Eba-175 Region II (Rii) Crystallized in the Presence of (Alpha)2,3-Sialyllactose, PDB code: 1zro was solved by N.H.Tolia, E.J.Enemark, B.K.Sim, L.Joshua-Tor, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.62 / 2.25
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 145.745, 146.208, 214.739, 90.00, 90.00, 90.00
R / Rfree (%) 21.6 / 23.2

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Eba-175 Region II (Rii) Crystallized in the Presence of (Alpha)2,3-Sialyllactose (pdb code 1zro). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Crystal Structure of Eba-175 Region II (Rii) Crystallized in the Presence of (Alpha)2,3-Sialyllactose, PDB code: 1zro:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in 1zro

Go back to Chlorine Binding Sites List in 1zro
Chlorine binding site 1 out of 4 in the Crystal Structure of Eba-175 Region II (Rii) Crystallized in the Presence of (Alpha)2,3-Sialyllactose


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 Eba-175 Region II (Rii) Crystallized in the Presence of (Alpha)2,3-Sialyllactose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl709

b:75.5
occ:1.00
NZ A:LYS150 3.7 53.9 1.0
NZ A:LYS61 4.0 45.0 1.0
CD A:LYS150 4.1 53.3 1.0
CE A:LYS150 4.2 54.1 1.0
CE A:LYS61 4.9 44.9 1.0

Chlorine binding site 2 out of 4 in 1zro

Go back to Chlorine Binding Sites List in 1zro
Chlorine binding site 2 out of 4 in the Crystal Structure of Eba-175 Region II (Rii) Crystallized in the Presence of (Alpha)2,3-Sialyllactose


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 Eba-175 Region II (Rii) Crystallized in the Presence of (Alpha)2,3-Sialyllactose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl710

b:86.0
occ:1.00
NH1 A:ARG437 3.5 67.1 1.0
O A:HOH787 3.9 45.7 1.0
O A:HOH935 4.2 66.0 1.0
CG2 A:THR430 4.2 43.0 1.0
NH2 A:ARG437 4.3 65.7 1.0
CZ A:ARG437 4.3 65.8 1.0
CB A:THR430 5.0 42.4 1.0
CA A:THR430 5.0 42.8 1.0

Chlorine binding site 3 out of 4 in 1zro

Go back to Chlorine Binding Sites List in 1zro
Chlorine binding site 3 out of 4 in the Crystal Structure of Eba-175 Region II (Rii) Crystallized in the Presence of (Alpha)2,3-Sialyllactose


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystal Structure of Eba-175 Region II (Rii) Crystallized in the Presence of (Alpha)2,3-Sialyllactose within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl719

b:75.5
occ:1.00
NZ B:LYS150 3.7 53.9 1.0
CD B:LYS150 4.0 53.3 1.0
NZ B:LYS61 4.1 45.0 1.0
CE B:LYS150 4.2 54.1 1.0
CE B:LYS61 4.9 44.9 1.0

Chlorine binding site 4 out of 4 in 1zro

Go back to Chlorine Binding Sites List in 1zro
Chlorine binding site 4 out of 4 in the Crystal Structure of Eba-175 Region II (Rii) Crystallized in the Presence of (Alpha)2,3-Sialyllactose


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Crystal Structure of Eba-175 Region II (Rii) Crystallized in the Presence of (Alpha)2,3-Sialyllactose within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl720

b:85.9
occ:1.00
NH1 B:ARG437 3.5 67.2 1.0
O B:HOH819 3.9 49.1 1.0
CG2 B:THR430 4.2 42.9 1.0
NH2 B:ARG437 4.3 65.7 1.0
CZ B:ARG437 4.4 65.9 1.0
O B:HOH968 4.4 69.8 1.0
CB B:THR430 4.9 42.3 1.0
CA B:THR430 5.0 42.7 1.0

Reference:

N.H.Tolia, E.J.Enemark, B.K.Sim, L.Joshua-Tor. Structural Basis For the Eba-175 Erythrocyte Invasion Pathway of the Malaria Parasite Plasmodium Falciparum. Cell(Cambridge,Mass.) V. 122 183 2005.
ISSN: ISSN 0092-8674
PubMed: 16051144
DOI: 10.1016/J.CELL.2005.05.033
Page generated: Sat Dec 12 08:57:25 2020

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