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Calcium in PDB 3ela: Crystal Structure of Active Site Inhibited Coagulation Factor Viia Mutant in Complex with Soluble Tissue Factor

Enzymatic activity of Crystal Structure of Active Site Inhibited Coagulation Factor Viia Mutant in Complex with Soluble Tissue Factor

All present enzymatic activity of Crystal Structure of Active Site Inhibited Coagulation Factor Viia Mutant in Complex with Soluble Tissue Factor:
3.4.21.21;

Protein crystallography data

The structure of Crystal Structure of Active Site Inhibited Coagulation Factor Viia Mutant in Complex with Soluble Tissue Factor, PDB code: 3ela was solved by J.R.Bjelke, M.Fodje, L.A.Svensson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.19 / 2.20
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 78.361, 68.558, 78.817, 90.00, 90.22, 90.00
R / Rfree (%) 23.3 / 29.4

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of Active Site Inhibited Coagulation Factor Viia Mutant in Complex with Soluble Tissue Factor (pdb code 3ela). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Crystal Structure of Active Site Inhibited Coagulation Factor Viia Mutant in Complex with Soluble Tissue Factor, PDB code: 3ela:

Calcium binding site 1 out of 1 in 3ela

Go back to Calcium Binding Sites List in 3ela
Calcium binding site 1 out of 1 in the Crystal Structure of Active Site Inhibited Coagulation Factor Viia Mutant in Complex with Soluble Tissue Factor


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of Active Site Inhibited Coagulation Factor Viia Mutant in Complex with Soluble Tissue Factor within 5.0Å range:
probe atom residue distance (Å) B Occ
H:Ca1

b:50.3
occ:1.00
 OE1 H:GLU210 2.2 22.2 1.0
O H:HOH484 2.3 29.2 1.0
OE2 H:GLU220 2.5 34.8 1.0
O H:GLU215 2.6 36.6 1.0
O H:HOH468 2.6 18.9 1.0
O H:ASP212 2.7 29.3 1.0
CD H:GLU210 3.3 21.5 1.0
C H:ASP212 3.4 28.2 1.0
N H:ASP212 3.4 27.2 1.0
CD H:GLU220 3.6 33.1 1.0
OE2 H:GLU210 3.6 19.8 1.0
O H:HOH487 3.7 22.1 1.0
C H:GLU215 3.7 36.4 1.0
CA H:ASP212 3.8 26.9 1.0
OD1 H:ASP217 3.9 35.6 1.0
CB H:ASP212 4.1 26.5 1.0
CG H:GLU220 4.1 28.8 1.0
N H:HIS211 4.1 23.8 1.0
N H:ASP217 4.1 35.4 1.0
CA H:HIS216 4.3 37.3 1.0
N H:LEU213 4.4 28.6 1.0
N H:HIS216 4.4 36.6 1.0
C H:HIS211 4.5 26.3 1.0
CG H:ASP217 4.5 35.6 1.0
CG H:GLU210 4.6 20.8 1.0
C H:HIS216 4.6 36.3 1.0
CG H:GLU215 4.7 36.1 1.0
OE1 H:GLU220 4.7 36.1 1.0
CA H:HIS211 4.7 25.5 1.0
N H:GLU215 4.8 35.5 1.0
CA H:GLU215 4.8 35.8 1.0
CA H:GLU210 4.8 20.9 1.0
CB H:ASP217 4.9 34.4 1.0
C H:GLU210 4.9 22.7 1.0
CA H:LEU213 5.0 29.8 1.0
CB H:HIS211 5.0 25.1 1.0

Reference:

J.R.Bjelke, O.H.Olsen, M.Fodje, L.A.Svensson, S.Bang, G.Bolt, B.B.Kragelund, E.Persson. Mechanism of the CA2+-Induced Enhancement of the Intrinsic Factor Viia Activity J.Biol.Chem. V. 283 25863 2008.
ISSN: ISSN 0021-9258
PubMed: 18640965
DOI: 10.1074/JBC.M800841200
Page generated: Sat Jul 13 09:30:39 2024

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