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Calcium in PDB 2fx4: Bovine Trypsin Bound By 4-Piperidinebutyrate to Make Acylenzyme Complex

Enzymatic activity of Bovine Trypsin Bound By 4-Piperidinebutyrate to Make Acylenzyme Complex

All present enzymatic activity of Bovine Trypsin Bound By 4-Piperidinebutyrate to Make Acylenzyme Complex:
3.4.21.4;

Protein crystallography data

The structure of Bovine Trypsin Bound By 4-Piperidinebutyrate to Make Acylenzyme Complex, PDB code: 2fx4 was solved by B.A.Katz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 7.00 / 1.65
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 63.940, 63.210, 69.670, 90.00, 90.00, 90.00
R / Rfree (%) 18.8 / 19.8

Calcium Binding Sites:

The binding sites of Calcium atom in the Bovine Trypsin Bound By 4-Piperidinebutyrate to Make Acylenzyme Complex (pdb code 2fx4). 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 Bovine Trypsin Bound By 4-Piperidinebutyrate to Make Acylenzyme Complex, PDB code: 2fx4:

Calcium binding site 1 out of 1 in 2fx4

Go back to Calcium Binding Sites List in 2fx4
Calcium binding site 1 out of 1 in the Bovine Trypsin Bound By 4-Piperidinebutyrate to Make Acylenzyme Complex


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Bovine Trypsin Bound By 4-Piperidinebutyrate to Make Acylenzyme Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca247

b:23.2
occ:1.00
O A:VAL75 2.2 13.2 1.0
O A:ASN72 2.2 12.0 1.0
O A:HOH248 2.3 15.3 1.0
O A:HOH560 2.3 15.5 1.0
OE2 A:GLU70 2.4 13.0 1.0
OE2 A:GLU80 2.4 13.4 1.0
C A:VAL75 3.3 15.8 1.0
CD A:GLU70 3.3 14.3 1.0
C A:ASN72 3.4 14.6 1.0
CD A:GLU80 3.5 14.3 1.0
OE1 A:GLU70 3.7 14.4 1.0
CG A:GLU80 3.9 13.8 1.0
CA A:VAL76 4.0 16.5 1.0
N A:VAL76 4.1 15.1 1.0
N A:VAL75 4.1 16.4 1.0
CA A:ILE73 4.2 15.1 1.0
N A:GLU77 4.2 15.9 1.0
N A:ILE73 4.2 14.5 1.0
CA A:VAL75 4.3 17.0 1.0
N A:ASN72 4.3 14.3 1.0
OE2 A:GLU77 4.3 16.8 1.0
CA A:ASN72 4.4 14.3 1.0
O A:HOH381 4.4 14.6 1.0
C A:ILE73 4.4 14.6 1.0
CG A:GLU77 4.5 16.3 1.0
OE1 A:GLU80 4.5 15.2 1.0
C A:VAL76 4.5 18.1 1.0
CB A:ASN72 4.6 15.0 1.0
N A:ASP71 4.7 13.8 1.0
CG A:GLU70 4.7 12.7 1.0
N A:ASN74 4.7 15.7 1.0
O A:ILE73 4.8 14.9 1.0
CD A:GLU77 4.9 19.6 1.0
CB A:GLU70 4.9 11.5 1.0
CA A:GLU70 4.9 10.5 1.0
CB A:VAL75 4.9 17.9 1.0
CB A:GLU77 4.9 15.7 1.0

Reference:

M.E.Mcgrath, P.A.Sprengeler, B.Hirschbein, J.R.Somoza, I.Lehoux, J.W.Janc, E.Gjerstad, M.Graupe, A.Estiarte, C.Venkataramani, Y.Liu, R.Yee, J.D.Ho, M.J.Green, C.-S.Lee, L.Liu, V.Tai, J.Spencer, D.Sperandio, B.A.Katz. Structure-Guided Design of Peptide-Based Tryptase Inhibitors. Biochemistry V. 45 5964 2006.
ISSN: ISSN 0006-2960
PubMed: 16681368
DOI: 10.1021/BI060173M
Page generated: Fri Jul 12 10:38:12 2024

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