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Calcium in PDB 1e8v: Structure of the Multifunctional Paramyxovirus Hemagglutinin- Neuraminidase

Enzymatic activity of Structure of the Multifunctional Paramyxovirus Hemagglutinin- Neuraminidase

All present enzymatic activity of Structure of the Multifunctional Paramyxovirus Hemagglutinin- Neuraminidase:
3.2.1.18;

Protein crystallography data

The structure of Structure of the Multifunctional Paramyxovirus Hemagglutinin- Neuraminidase, PDB code: 1e8v was solved by S.Crennell, T.Takimoto, A.Portner, G.Taylor, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 6.00 / 2.00
Space group P 61
Cell size a, b, c (Å), α, β, γ (°) 137.460, 137.460, 116.600, 90.00, 90.00, 120.00
R / Rfree (%) 23.2 / 26.7

Calcium Binding Sites:

The binding sites of Calcium atom in the Structure of the Multifunctional Paramyxovirus Hemagglutinin- Neuraminidase (pdb code 1e8v). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Structure of the Multifunctional Paramyxovirus Hemagglutinin- Neuraminidase, PDB code: 1e8v:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 1e8v

Go back to Calcium Binding Sites List in 1e8v
Calcium binding site 1 out of 2 in the Structure of the Multifunctional Paramyxovirus Hemagglutinin- Neuraminidase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure of the Multifunctional Paramyxovirus Hemagglutinin- Neuraminidase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca1001

b:57.4
occ:1.00
O A:VAL266 2.2 55.7 1.0
O A:SER264 2.4 59.8 1.0
O A:VAL296 2.4 53.4 1.0
O A:ASP261 2.5 59.1 1.0
OD1 A:ASP261 2.5 59.7 1.0
OG A:SER264 2.7 58.2 1.0
C A:SER264 3.4 59.1 1.0
C A:VAL266 3.4 56.1 1.0
C A:ASP261 3.5 60.5 1.0
CB A:SER264 3.5 58.6 1.0
CG A:ASP261 3.6 59.2 1.0
C A:VAL296 3.7 52.7 1.0
OE2 A:GLU256 3.8 60.9 1.0
CA A:ASP261 3.9 60.7 1.0
CA A:SER264 3.9 58.9 1.0
N A:VAL266 3.9 57.4 1.0
CA A:VAL266 4.2 57.0 1.0
CB A:ASP261 4.3 60.0 1.0
C A:PRO267 4.3 53.1 1.0
N A:SER264 4.4 59.4 1.0
O A:PRO267 4.4 53.4 1.0
N A:PRO267 4.4 55.1 1.0
OD2 A:ASP261 4.5 59.3 1.0
C A:ALA265 4.5 58.3 1.0
N A:ALA265 4.5 58.7 1.0
CA A:VAL296 4.5 51.7 1.0
CA A:PRO267 4.6 54.0 1.0
N A:ALA297 4.6 53.3 1.0
N A:TYR262 4.7 60.9 1.0
N A:THR268 4.7 52.3 1.0
CA A:ALA297 4.7 53.0 1.0
CB A:VAL266 4.7 57.4 1.0
CG2 A:VAL266 4.8 57.6 1.0
OG1 A:THR268 4.8 50.2 1.0
CD A:GLU256 4.9 61.2 1.0
CA A:ALA265 4.9 58.4 1.0

Calcium binding site 2 out of 2 in 1e8v

Go back to Calcium Binding Sites List in 1e8v
Calcium binding site 2 out of 2 in the Structure of the Multifunctional Paramyxovirus Hemagglutinin- Neuraminidase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Structure of the Multifunctional Paramyxovirus Hemagglutinin- Neuraminidase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca1002

b:63.7
occ:1.00
O B:VAL266 2.2 54.9 1.0
OD1 B:ASP261 2.4 58.9 1.0
O B:SER264 2.5 59.4 1.0
O B:VAL296 2.5 53.9 1.0
O B:ASP261 2.6 59.2 1.0
OG B:SER264 2.7 59.2 1.0
C B:VAL266 3.4 55.7 1.0
C B:SER264 3.5 58.9 1.0
CG B:ASP261 3.5 59.2 1.0
C B:ASP261 3.5 60.6 1.0
CB B:SER264 3.6 58.8 1.0
OE2 B:GLU256 3.7 60.5 1.0
C B:VAL296 3.8 53.0 1.0
CA B:ASP261 3.9 60.6 1.0
N B:VAL266 4.0 56.7 1.0
CA B:SER264 4.0 59.0 1.0
CA B:VAL266 4.2 56.6 1.0
O B:PRO267 4.2 53.4 1.0
C B:PRO267 4.2 53.4 1.0
CB B:ASP261 4.3 59.8 1.0
N B:PRO267 4.4 54.9 1.0
OD2 B:ASP261 4.4 59.1 1.0
N B:SER264 4.5 59.8 1.0
CA B:PRO267 4.5 54.2 1.0
C B:ALA265 4.6 57.5 1.0
N B:THR268 4.6 52.3 1.0
N B:ALA265 4.6 58.6 1.0
CB B:VAL266 4.7 57.3 1.0
CA B:VAL296 4.7 51.8 1.0
N B:ALA297 4.7 53.3 1.0
CG2 B:VAL266 4.7 58.0 1.0
CA B:ALA297 4.7 52.8 1.0
OG1 B:THR268 4.8 50.2 1.0
N B:TYR262 4.8 60.9 1.0
CD B:GLU256 4.8 60.2 1.0

Reference:

S.Crennell, T.Takimoto, A.Portner, G.Taylor. Crystal Structure of the Multifunctional Paramyxovirus Hemagglutinin-Neuraminidase Nat.Struct.Biol. V. 7 1068 2000.
ISSN: ISSN 1072-8368
PubMed: 11062565
DOI: 10.1038/81002
Page generated: Mon Jul 7 14:35:36 2025

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