Calcium in PDB 6d05: Cryo-Em Structure of A Plasmodium Vivax Invasion Complex Essential For Entry Into Human Reticulocytes; Two Molecules of Parasite Ligand, Subclass 2.

Other elements in 6d05:

The structure of Cryo-Em Structure of A Plasmodium Vivax Invasion Complex Essential For Entry Into Human Reticulocytes; Two Molecules of Parasite Ligand, Subclass 2. also contains other interesting chemical elements:

Iron (Fe) 4 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Cryo-Em Structure of A Plasmodium Vivax Invasion Complex Essential For Entry Into Human Reticulocytes; Two Molecules of Parasite Ligand, Subclass 2. (pdb code 6d05). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Cryo-Em Structure of A Plasmodium Vivax Invasion Complex Essential For Entry Into Human Reticulocytes; Two Molecules of Parasite Ligand, Subclass 2., PDB code: 6d05:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 6d05

Go back to Calcium Binding Sites List in 6d05
Calcium binding site 1 out of 2 in the Cryo-Em Structure of A Plasmodium Vivax Invasion Complex Essential For Entry Into Human Reticulocytes; Two Molecules of Parasite Ligand, Subclass 2.


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Cryo-Em Structure of A Plasmodium Vivax Invasion Complex Essential For Entry Into Human Reticulocytes; Two Molecules of Parasite Ligand, Subclass 2. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca801

b:50.5
occ:1.00
O A:THR310 2.4 48.6 1.0
O A:PHE313 2.4 46.4 1.0
OE2 A:GLU465 2.4 41.9 1.0
OE1 A:GLU468 2.5 42.5 1.0
OG1 A:THR310 2.8 48.6 1.0
CD A:GLU465 3.3 41.9 1.0
C A:PHE313 3.4 46.4 1.0
OE1 A:GLU465 3.5 41.9 1.0
C A:THR310 3.6 48.6 1.0
CB A:THR310 3.6 48.6 1.0
CD A:GLU468 3.7 42.5 1.0
CA A:PRO314 3.9 44.2 1.0
N A:PHE313 4.1 46.4 1.0
N A:PRO314 4.1 44.2 1.0
OG A:SER315 4.2 46.5 1.0
CA A:THR310 4.2 48.6 1.0
N A:GLY312 4.3 48.3 1.0
O A:ASP307 4.3 54.5 1.0
C A:PRO314 4.4 44.2 1.0
OE2 A:GLU468 4.4 42.5 1.0
CA A:PHE313 4.4 46.4 1.0
N A:SER315 4.5 46.5 1.0
N A:PRO311 4.6 51.8 1.0
CB A:GLU468 4.6 42.5 1.0
CG A:GLU465 4.6 41.9 1.0
C A:PRO311 4.6 51.8 1.0
C A:GLY312 4.7 48.3 1.0
CA A:PRO311 4.7 51.8 1.0
CB A:ASP307 4.7 54.5 1.0
CG A:GLU468 4.8 42.5 1.0
N A:ASP307 4.9 54.5 1.0
CG2 A:THR310 5.0 48.6 1.0
N A:THR310 5.0 48.6 1.0
CA A:GLY312 5.0 48.3 1.0

Calcium binding site 2 out of 2 in 6d05

Go back to Calcium Binding Sites List in 6d05
Calcium binding site 2 out of 2 in the Cryo-Em Structure of A Plasmodium Vivax Invasion Complex Essential For Entry Into Human Reticulocytes; Two Molecules of Parasite Ligand, Subclass 2.


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Cryo-Em Structure of A Plasmodium Vivax Invasion Complex Essential For Entry Into Human Reticulocytes; Two Molecules of Parasite Ligand, Subclass 2. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca801

b:44.7
occ:1.00
OE2 B:GLU465 2.4 44.1 1.0
O B:THR310 2.4 50.4 1.0
OE1 B:GLU468 2.5 45.5 1.0
O B:PHE313 2.6 47.5 1.0
OG1 B:THR310 2.9 50.4 1.0
CD B:GLU465 3.3 44.1 1.0
C B:THR310 3.6 50.4 1.0
C B:PHE313 3.6 47.5 1.0
OE1 B:GLU465 3.6 44.1 1.0
CD B:GLU468 3.7 45.5 1.0
CB B:THR310 3.7 50.4 1.0
CA B:PRO314 4.1 45.4 1.0
N B:PHE313 4.2 47.5 1.0
O B:ASP307 4.2 57.1 1.0
N B:PRO314 4.3 45.4 1.0
N B:GLY312 4.3 51.0 1.0
CA B:THR310 4.3 50.4 1.0
OG B:SER315 4.3 48.5 1.0
OE2 B:GLU468 4.3 45.5 1.0
CA B:PHE313 4.5 47.5 1.0
N B:PRO311 4.6 54.3 1.0
C B:PRO314 4.6 45.4 1.0
CB B:GLU468 4.6 45.5 1.0
CG B:GLU465 4.6 44.1 1.0
C B:PRO311 4.6 54.3 1.0
CA B:PRO311 4.6 54.3 1.0
N B:SER315 4.6 48.5 1.0
CB B:ASP307 4.7 57.1 1.0
C B:GLY312 4.7 51.0 1.0
CG B:GLU468 4.7 45.5 1.0
N B:ASP307 4.8 57.1 1.0
CA B:GLY312 5.0 51.0 1.0

Reference:

J.Gruszczyk, R.K.Huang, L.J.Chan, S.Menant, C.Hong, J.M.Murphy, Y.F.Mok, M.D.W.Griffin, R.D.Pearson, W.Wong, A.F.Cowman, Z.Yu, W.H.Tham. Cryo-Em Structure of An Essential Plasmodium Vivax Invasion Complex. Nature V. 559 135 2018.
ISSN: ISSN 0028-0836
PubMed: 29950717
DOI: 10.1038/S41586-018-0249-1
Page generated: Sat Dec 12 06:02:13 2020

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