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Calcium in PDB 5jbb: Crystal Structure of Factor Ixa Variant V16I K98T Y177T I213V in Complex with Egr-Chloromethylketone

Enzymatic activity of Crystal Structure of Factor Ixa Variant V16I K98T Y177T I213V in Complex with Egr-Chloromethylketone

All present enzymatic activity of Crystal Structure of Factor Ixa Variant V16I K98T Y177T I213V in Complex with Egr-Chloromethylketone:
3.4.21.22;

Protein crystallography data

The structure of Crystal Structure of Factor Ixa Variant V16I K98T Y177T I213V in Complex with Egr-Chloromethylketone, PDB code: 5jbb was solved by L.H.Kristensen, H.Brandstetter, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 21.60 / 1.56
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 44.310, 66.610, 97.050, 90.00, 90.00, 90.00
R / Rfree (%) 15.8 / 19

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of Factor Ixa Variant V16I K98T Y177T I213V in Complex with Egr-Chloromethylketone (pdb code 5jbb). 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 Factor Ixa Variant V16I K98T Y177T I213V in Complex with Egr-Chloromethylketone, PDB code: 5jbb:

Calcium binding site 1 out of 1 in 5jbb

Go back to Calcium Binding Sites List in 5jbb
Calcium binding site 1 out of 1 in the Crystal Structure of Factor Ixa Variant V16I K98T Y177T I213V in Complex with Egr-Chloromethylketone


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 Factor Ixa Variant V16I K98T Y177T I213V in Complex with Egr-Chloromethylketone within 5.0Å range:
probe atom residue distance (Å) B Occ
S:Ca301

b:18.5
occ:1.00
 OE1 S:GLU70 2.3 18.2 1.0
O S:GLU75 2.3 18.9 1.0
O S:ASN72 2.3 23.0 1.0
OE2 S:GLU80 2.4 19.5 1.0
OE1 S:GLU77 2.4 21.9 1.0
O S:HOH434 2.4 22.4 1.0
OE2 S:GLU77 2.5 20.7 1.0
CD S:GLU77 2.7 22.0 1.0
H S:ASN72 3.3 22.8 1.0
C S:GLU75 3.4 20.0 1.0
CD S:GLU70 3.4 21.0 1.0
HA S:THR76 3.4 24.9 1.0
C S:ASN72 3.5 20.0 1.0
CD S:GLU80 3.5 19.5 1.0
HG2 S:GLU80 3.5 23.0 1.0
H S:HIS71 3.6 19.6 1.0
H S:GLU77 3.6 25.1 1.0
HA S:ILE73 3.7 27.6 1.0
H S:GLU75 3.7 26.3 1.0
OE2 S:GLU70 3.7 21.2 1.0
CG S:GLU80 3.9 19.1 1.0
N S:ASN72 3.9 19.0 1.0
HB3 S:ASN72 4.0 21.2 1.0
HG3 S:GLU80 4.0 23.0 1.0
CA S:THR76 4.1 20.8 1.0
N S:GLU77 4.1 20.9 1.0
N S:THR76 4.2 21.5 1.0
CA S:ASN72 4.2 18.5 1.0
CG S:GLU77 4.2 22.4 1.0
HB2 S:GLU77 4.3 23.8 1.0
N S:GLU75 4.3 21.9 1.0
HA S:GLU70 4.3 20.0 1.0
CA S:GLU75 4.4 23.9 1.0
CA S:ILE73 4.4 23.0 1.0
HB2 S:GLU75 4.4 26.4 1.0
N S:ILE73 4.4 18.6 1.0
N S:HIS71 4.4 16.3 1.0
C S:THR76 4.5 21.8 1.0
OE1 S:GLU80 4.6 20.6 1.0
CB S:ASN72 4.6 17.7 1.0
HG2 S:GLU77 4.7 26.9 1.0
CB S:GLU77 4.7 19.9 1.0
CG S:GLU70 4.7 21.2 1.0
HG3 S:GLU77 4.7 26.9 1.0
HG3 S:GLU70 4.8 25.5 1.0
C S:ILE73 4.8 23.1 1.0
HB3 S:HIS71 4.9 22.7 1.0
CB S:GLU75 4.9 22.0 1.0
C S:HIS71 4.9 20.1 1.0
H S:THR76 5.0 25.8 1.0

Reference:

L.H.Kristensen, O.H.Olsen, G.E.Blouse, H.Brandstetter. Releasing the Brakes in Coagulation Factor Ixa By Co-Operative Maturation of the Substrate-Binding Site. Biochem.J. V. 473 2395 2016.
ISSN: ESSN 1470-8728
PubMed: 27208168
DOI: 10.1042/BCJ20160336
Page generated: Mon Jul 15 06:25:05 2024

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