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Calcium in PDB 1bc3: Recombinant Rat Annexin V, Triple Mutant (T72K, S144K, S228K)

Protein crystallography data

The structure of Recombinant Rat Annexin V, Triple Mutant (T72K, S144K, S228K), PDB code: 1bc3 was solved by Y.D.Mo, M.A.Swairjo, C.W.Li, J.F.Head, B.A.Seaton, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.95
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 157.340, 157.340, 37.590, 90.00, 90.00, 120.00
R / Rfree (%) 25.9 / 21.1

Calcium Binding Sites:

The binding sites of Calcium atom in the Recombinant Rat Annexin V, Triple Mutant (T72K, S144K, S228K) (pdb code 1bc3). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 5 binding sites of Calcium where determined in the Recombinant Rat Annexin V, Triple Mutant (T72K, S144K, S228K), PDB code: 1bc3:
Jump to Calcium binding site number: 1; 2; 3; 4; 5;

Calcium binding site 1 out of 5 in 1bc3

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Calcium binding site 1 out of 5 in the Recombinant Rat Annexin V, Triple Mutant (T72K, S144K, S228K)


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Recombinant Rat Annexin V, Triple Mutant (T72K, S144K, S228K) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca401

b:3.9
occ:1.00
O A:GLY28 2.6 49.1 1.0
O A:GLY30 2.7 32.1 1.0
O A:MET26 2.7 26.3 1.0
OE2 A:GLU70 2.7 40.8 1.0
OE1 A:GLU70 2.7 38.5 1.0
O A:HOH599 2.7 46.0 1.0
O A:HOH525 2.9 44.4 1.0
CD A:GLU70 3.1 39.2 1.0
C A:GLY30 3.7 36.2 1.0
N A:GLY30 3.8 45.5 1.0
C A:MET26 3.8 26.8 1.0
C A:GLY28 3.8 49.1 1.0
OG1 A:THR31 4.2 30.3 1.0
CA A:GLY30 4.3 41.2 1.0
C A:LEU29 4.3 47.7 1.0
CA A:MET26 4.5 23.7 1.0
CA A:LEU29 4.5 49.0 1.0
CG A:GLU70 4.6 36.4 1.0
C A:LYS27 4.6 42.2 1.0
N A:GLY28 4.6 44.1 1.0
N A:LEU29 4.6 50.1 1.0
O A:HOH574 4.7 23.0 1.0
N A:THR31 4.7 34.4 1.0
O A:LYS27 4.7 41.4 1.0
CA A:GLY28 4.8 48.4 1.0
N A:LYS27 4.8 33.0 1.0
O A:HOH555 4.9 30.8 1.0
O A:LEU29 5.0 49.5 1.0
CA A:THR31 5.0 30.6 1.0

Calcium binding site 2 out of 5 in 1bc3

Go back to Calcium Binding Sites List in 1bc3
Calcium binding site 2 out of 5 in the Recombinant Rat Annexin V, Triple Mutant (T72K, S144K, S228K)


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Recombinant Rat Annexin V, Triple Mutant (T72K, S144K, S228K) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca402

b:27.6
occ:1.00
O A:LYS68 2.7 27.1 1.0
OE2 A:GLU76 2.9 35.1 1.0
O A:HOH600 2.9 53.7 1.0
O A:LEU71 3.1 32.6 1.0
C A:LYS68 3.9 26.0 1.0
CD A:GLU76 4.0 28.3 1.0
C A:LEU71 4.3 30.6 1.0
CA A:LYS72 4.6 34.4 1.0
CG A:LYS72 4.8 50.2 1.0
CG A:GLU76 4.8 26.0 1.0
CA A:LYS68 4.8 20.2 1.0
CA A:SER69 4.8 29.1 1.0
N A:SER69 4.9 27.9 1.0
N A:LYS72 4.9 32.5 1.0
OE1 A:GLU76 4.9 38.8 1.0

Calcium binding site 3 out of 5 in 1bc3

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Calcium binding site 3 out of 5 in the Recombinant Rat Annexin V, Triple Mutant (T72K, S144K, S228K)


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of Recombinant Rat Annexin V, Triple Mutant (T72K, S144K, S228K) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca407

b:2.0
occ:1.00
O A:LYS184 2.6 12.1 1.0
O A:GLY181 2.6 8.8 1.0
O A:GLY186 2.6 15.0 1.0
OE1 A:GLU226 2.7 16.4 1.0
OE2 A:GLU226 2.8 16.8 1.0
O A:HOH603 2.9 12.2 1.0
CD A:GLU226 3.1 17.1 1.0
C A:GLY181 3.5 9.1 1.0
C A:GLY186 3.7 13.7 1.0
C A:LYS184 3.7 10.7 1.0
N A:GLY186 3.8 13.1 1.0
CA A:GLY186 4.3 12.0 1.0
CA A:GLY181 4.3 7.1 1.0
N A:LYS184 4.4 12.9 1.0
N A:GLU182 4.4 8.4 1.0
OG1 A:THR187 4.4 16.6 1.0
CA A:LYS184 4.4 12.0 1.0
O A:GLU182 4.4 10.8 1.0
CA A:GLU182 4.5 8.9 1.0
O A:HOH507 4.5 17.9 1.0
C A:GLU182 4.6 10.0 1.0
CG A:GLU226 4.6 13.7 1.0
C A:TRP185 4.6 11.0 1.0
CB A:LYS184 4.6 10.1 1.0
N A:TRP185 4.7 9.5 1.0
N A:THR187 4.7 12.7 1.0
CA A:TRP185 4.7 7.0 1.0
CA A:THR187 4.9 11.3 1.0

Calcium binding site 4 out of 5 in 1bc3

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Calcium binding site 4 out of 5 in the Recombinant Rat Annexin V, Triple Mutant (T72K, S144K, S228K)


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 4 of Recombinant Rat Annexin V, Triple Mutant (T72K, S144K, S228K) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca408

b:14.7
occ:1.00
O A:ASP224 2.8 13.4 1.0
O A:THR227 2.9 17.7 1.0
OD1 A:ASP224 3.0 33.5 1.0
O A:HOH608 3.0 57.9 1.0
OE1 A:GLU232 3.0 19.6 1.0
CD A:GLU232 3.3 20.3 1.0
OE2 A:GLU232 3.4 28.4 1.0
C A:ASP224 3.8 17.4 1.0
CG A:ASP224 4.0 30.8 1.0
CA A:ASP224 4.0 13.9 1.0
C A:THR227 4.1 19.9 1.0
CA A:LYS228 4.2 27.3 1.0
CG A:GLU232 4.3 14.0 1.0
CB A:LYS228 4.4 31.0 1.0
CB A:ASP224 4.6 23.2 1.0
N A:LYS228 4.6 23.8 1.0
OD2 A:ASP224 4.8 37.7 1.0
O A:ILE223 4.9 11.1 1.0

Calcium binding site 5 out of 5 in 1bc3

Go back to Calcium Binding Sites List in 1bc3
Calcium binding site 5 out of 5 in the Recombinant Rat Annexin V, Triple Mutant (T72K, S144K, S228K)


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 5 of Recombinant Rat Annexin V, Triple Mutant (T72K, S144K, S228K) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca410

b:30.5
occ:1.00
O A:GLY261 2.8 68.4 1.0
OD2 A:ASP301 2.9 46.6 1.0
O A:HOH609 2.9 58.1 1.0
OD1 A:ASP301 2.9 47.5 1.0
O A:MET257 3.0 60.9 1.0
O A:LYS258 3.0 96.4 1.0
O A:GLY259 3.1 98.6 1.0
CG A:ASP301 3.3 46.1 1.0
N A:GLY261 3.3 80.8 1.0
C A:GLY259 3.5 96.6 1.0
CA A:ALA260 3.6 90.8 1.0
C A:ALA260 3.6 86.5 1.0
N A:ALA260 3.8 94.9 1.0
C A:GLY261 3.8 66.9 1.0
C A:LYS258 3.9 91.4 1.0
C A:MET257 4.0 60.3 1.0
CA A:GLY261 4.1 73.8 1.0
O A:ALA260 4.5 87.3 1.0
CA A:GLY259 4.6 96.7 1.0
N A:GLY259 4.6 94.5 1.0
CB A:ASP301 4.8 43.2 1.0
N A:LYS258 4.8 72.9 1.0
OG1 A:THR262 4.8 39.8 1.0
CA A:LYS258 4.9 85.3 1.0
CA A:MET257 4.9 50.8 1.0
N A:THR262 5.0 56.9 1.0
CB A:ALA260 5.0 93.5 1.0

Reference:

B.Campos, Y.D.Mo, T.R.Mealy, C.W.Li, M.A.Swairjo, C.Balch, J.F.Head, G.Retzinger, J.R.Dedman, B.A.Seaton. Mutational and Crystallographic Analyses of Interfacial Residues in Annexin V Suggest Direct Interactions with Phospholipid Membrane Components. Biochemistry V. 37 8004 1998.
ISSN: ISSN 0006-2960
PubMed: 9609693
DOI: 10.1021/BI973142N
Page generated: Thu Jul 11 06:20:18 2024

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