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Calcium in PDB 1gi4: A Novel Serine Protease Inhibition Motif Involving A Multi-Centered Short Hydrogen Bonding Network at the Active Site

Enzymatic activity of A Novel Serine Protease Inhibition Motif Involving A Multi-Centered Short Hydrogen Bonding Network at the Active Site

All present enzymatic activity of A Novel Serine Protease Inhibition Motif Involving A Multi-Centered Short Hydrogen Bonding Network at the Active Site:
3.4.21.4;

Protein crystallography data

The structure of A Novel Serine Protease Inhibition Motif Involving A Multi-Centered Short Hydrogen Bonding Network at the Active Site, PDB code: 1gi4 was solved by B.A.Katz, K.Elrod, C.Luong, M.Rice, R.L.Mackman, P.A.Sprengeler, J.Spencer, J.Hatayte, J.Janc, J.Link, J.Litvak, R.Rai, K.Rice, S.Sideris, E.Verner, W.Young, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 7.00 / 1.37
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 63.660, 63.070, 68.990, 90.00, 90.00, 90.00
R / Rfree (%) 19.3 / 21.4

Other elements in 1gi4:

The structure of A Novel Serine Protease Inhibition Motif Involving A Multi-Centered Short Hydrogen Bonding Network at the Active Site also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the A Novel Serine Protease Inhibition Motif Involving A Multi-Centered Short Hydrogen Bonding Network at the Active Site (pdb code 1gi4). 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 A Novel Serine Protease Inhibition Motif Involving A Multi-Centered Short Hydrogen Bonding Network at the Active Site, PDB code: 1gi4:

Calcium binding site 1 out of 1 in 1gi4

Go back to Calcium Binding Sites List in 1gi4
Calcium binding site 1 out of 1 in the A Novel Serine Protease Inhibition Motif Involving A Multi-Centered Short Hydrogen Bonding Network at the Active Site


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of A Novel Serine Protease Inhibition Motif Involving A Multi-Centered Short Hydrogen Bonding Network at the Active Site within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca247

b:25.5
occ:1.00
O A:VAL75 2.1 13.8 1.0
O A:ASN72 2.2 13.4 1.0
O A:HOH248 2.3 14.7 1.0
O A:HOH560 2.3 14.5 1.0
OE2 A:GLU70 2.4 14.7 1.0
OE2 A:GLU80 2.4 14.5 1.0
H1 A:HOH560 3.0 14.2 1.0
H1 A:HOH248 3.0 14.3 1.0
HA A:VAL76 3.1 15.6 1.0
H2 A:HOH248 3.1 14.8 1.0
H2 A:HOH560 3.1 14.5 1.0
C A:VAL75 3.3 15.0 1.0
CD A:GLU70 3.3 16.2 1.0
C A:ASN72 3.4 14.4 1.0
H A:GLU77 3.4 15.6 1.0
HG2 A:GLU80 3.4 14.6 1.0
CD A:GLU80 3.5 15.1 1.0
H A:VAL75 3.5 15.4 1.0
HA A:ILE73 3.5 12.2 1.0
OE1 A:GLU70 3.6 15.3 1.0
H A:ASP71 3.7 14.0 1.0
HG3 A:GLU77 3.7 17.5 1.0
HB3 A:ASN72 3.7 14.4 1.0
CG A:GLU80 3.9 14.5 1.0
CA A:VAL76 3.9 15.5 1.0
HA A:GLU70 4.0 12.6 1.0
N A:VAL76 4.0 13.7 1.0
H A:ASN72 4.0 13.9 1.0
N A:VAL75 4.0 15.9 1.0
HG3 A:GLU80 4.0 14.7 1.0
N A:GLU77 4.1 15.1 1.0
CA A:ILE73 4.1 13.8 1.0
N A:ILE73 4.2 14.3 1.0
N A:ASN72 4.2 13.6 1.0
CA A:VAL75 4.2 15.9 1.0
CA A:ASN72 4.3 13.1 1.0
O A:HOH381 4.3 16.0 1.0
OE2 A:GLU77 4.4 17.5 1.0
C A:ILE73 4.4 14.4 1.0
HB A:VAL75 4.4 16.2 1.0
CB A:ASN72 4.5 14.7 1.0
OE1 A:GLU80 4.5 15.7 1.0
CG A:GLU77 4.5 17.4 1.0
C A:VAL76 4.5 17.0 1.0
HB2 A:GLU77 4.6 16.5 1.0
HB3 A:GLU70 4.6 12.6 1.0
N A:ASP71 4.6 14.6 1.0
N A:ASN74 4.7 15.6 1.0
H A:ASN74 4.7 17.1 1.0
CG A:GLU70 4.7 13.7 1.0
HG22 A:VAL76 4.7 17.0 1.0
O A:ILE73 4.8 15.1 1.0
CA A:GLU70 4.8 12.3 1.0
CD A:GLU77 4.9 19.8 1.0
CB A:GLU70 4.9 12.5 1.0
CB A:VAL75 4.9 16.7 1.0
CB A:GLU77 4.9 16.7 1.0
H1 A:HOH381 4.9 16.0 1.0
H A:VAL76 4.9 13.8 1.0
C A:ASP71 5.0 14.9 1.0
H2 A:HOH277 5.0 14.8 1.0

Reference:

B.A.Katz, K.Elrod, C.Luong, M.J.Rice, R.L.Mackman, P.A.Sprengeler, J.Spencer, J.Hataye, J.Janc, J.Link, J.Litvak, R.Rai, K.Rice, S.Sideris, E.Verner, W.Young. A Novel Serine Protease Inhibition Motif Involving A Multi-Centered Short Hydrogen Bonding Network at the Active Site. J.Mol.Biol. V. 307 1451 2001.
ISSN: ISSN 0022-2836
PubMed: 11292354
DOI: 10.1006/JMBI.2001.4516
Page generated: Sat Dec 12 02:57:51 2020

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