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Calcium in PDB 1o2p: Elaborate Manifold of Short Hydrogen Bond Arrays Mediating Binding of Active Site-Directed Serine Protease Inhibitors

Enzymatic activity of Elaborate Manifold of Short Hydrogen Bond Arrays Mediating Binding of Active Site-Directed Serine Protease Inhibitors

All present enzymatic activity of Elaborate Manifold of Short Hydrogen Bond Arrays Mediating Binding of Active Site-Directed Serine Protease Inhibitors:
3.4.21.4;

Protein crystallography data

The structure of Elaborate Manifold of Short Hydrogen Bond Arrays Mediating Binding of Active Site-Directed Serine Protease Inhibitors, PDB code: 1o2p was solved by B.A.Katz, K.Elrod, E.Verner, R.L.Mackman, C.Luong, W.Shrader, M.Sendzik, J.R.Spencer, P.A.Sprengeler, A.Kolesnikov, W.F.Tai, H.Hui, G.Breitenbucher, D.Allen, J.Janc, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 7.00 / 1.47
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 63.750, 63.520, 69.220, 90.00, 90.00, 90.00
R / Rfree (%) 19.4 / 20.5

Other elements in 1o2p:

The structure of Elaborate Manifold of Short Hydrogen Bond Arrays Mediating Binding of Active Site-Directed Serine Protease Inhibitors also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Elaborate Manifold of Short Hydrogen Bond Arrays Mediating Binding of Active Site-Directed Serine Protease Inhibitors (pdb code 1o2p). 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 Elaborate Manifold of Short Hydrogen Bond Arrays Mediating Binding of Active Site-Directed Serine Protease Inhibitors, PDB code: 1o2p:

Calcium binding site 1 out of 1 in 1o2p

Go back to Calcium Binding Sites List in 1o2p
Calcium binding site 1 out of 1 in the Elaborate Manifold of Short Hydrogen Bond Arrays Mediating Binding of Active Site-Directed Serine Protease Inhibitors


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Elaborate Manifold of Short Hydrogen Bond Arrays Mediating Binding of Active Site-Directed Serine Protease Inhibitors within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca247

b:30.8
occ:1.00
O A:VAL75 2.1 12.1 1.0
O A:ASN72 2.2 11.6 1.0
O A:HOH248 2.3 16.3 1.0
O A:HOH560 2.3 16.8 1.0
OE2 A:GLU70 2.4 13.4 1.0
OE2 A:GLU80 2.5 14.3 1.0
H1 A:HOH248 3.0 17.8 1.0
H1 A:HOH560 3.0 16.7 1.0
H2 A:HOH248 3.1 18.3 1.0
H2 A:HOH560 3.1 17.5 1.0
HA A:VAL76 3.2 16.6 1.0
C A:VAL75 3.3 15.7 1.0
H A:VAL75 3.4 16.4 1.0
C A:ASN72 3.4 15.9 1.0
CD A:GLU70 3.4 13.3 1.0
HA A:ILE73 3.4 14.3 1.0
H A:GLU77 3.5 18.9 1.0
HG3 A:GLU77 3.5 18.3 1.0
CD A:GLU80 3.5 14.3 1.0
HG2 A:GLU80 3.6 14.6 1.0
OE1 A:GLU70 3.6 13.8 1.0
H A:ASP71 3.7 13.9 1.0
HB3 A:ASN72 3.8 16.1 1.0
N A:VAL75 4.0 15.6 1.0
CA A:VAL76 4.0 17.0 1.0
N A:VAL76 4.0 15.2 1.0
CG A:GLU80 4.0 15.0 1.0
HA A:GLU70 4.1 11.0 1.0
H A:ASN72 4.1 15.8 1.0
HG3 A:GLU80 4.1 14.7 1.0
CA A:ILE73 4.1 15.8 1.0
N A:ILE73 4.2 15.1 1.0
N A:GLU77 4.2 17.5 1.0
CA A:VAL75 4.2 16.4 1.0
N A:ASN72 4.3 13.2 1.0
CA A:ASN72 4.3 14.1 1.0
OE2 A:GLU77 4.3 18.3 1.0
HB A:VAL75 4.3 16.1 1.0
C A:ILE73 4.4 14.7 1.0
O A:HOH381 4.4 12.8 1.0
CG A:GLU77 4.4 17.8 1.0
CB A:ASN72 4.5 15.6 1.0
HB3 A:GLU70 4.5 10.4 1.0
C A:VAL76 4.5 18.8 1.0
OE1 A:GLU80 4.6 14.6 1.0
N A:ASN74 4.7 16.0 1.0
N A:ASP71 4.7 15.3 1.0
HB2 A:GLU77 4.7 17.7 1.0
H A:ASN74 4.7 17.1 1.0
CG A:GLU70 4.7 11.7 1.0
O A:ILE73 4.8 15.0 1.0
CB A:VAL75 4.8 16.0 1.0
CD A:GLU77 4.8 20.2 1.0
CB A:GLU70 4.9 11.4 1.0
CA A:GLU70 4.9 10.2 1.0
HG22 A:VAL76 4.9 14.9 1.0
H A:VAL76 4.9 17.7 1.0
CB A:GLU77 5.0 18.0 1.0
C A:ASP71 5.0 16.3 1.0

Reference:

B.A.Katz, K.Elrod, E.Verner, R.L.Mackman, C.Luong, W.D.Shrader, M.Sendzik, J.R.Spencer, P.A.Sprengeler, A.Kolesnikov, V.W.-F.Tai, H.C.Hui, J.G.Breitenbucher, D.Allen, J.W.Janc. Elaborate Manifold of Short Hydrogen Bond Arrays Mediating Binding of Active Site-Directed Serine Protease Inhibitors J.Mol.Biol. V. 329 93 2003.
ISSN: ISSN 0022-2836
PubMed: 12742021
DOI: 10.1016/S0022-2836(03)00399-1
Page generated: Thu Jul 11 13:11:03 2024

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