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Calcium in PDB 4hgc: Crystal Structure of Bovine Trypsin Complexed with Sfti-1 Analog Containing A Peptoid Residue at Position P1

Enzymatic activity of Crystal Structure of Bovine Trypsin Complexed with Sfti-1 Analog Containing A Peptoid Residue at Position P1

All present enzymatic activity of Crystal Structure of Bovine Trypsin Complexed with Sfti-1 Analog Containing A Peptoid Residue at Position P1:
3.4.21.4;

Protein crystallography data

The structure of Crystal Structure of Bovine Trypsin Complexed with Sfti-1 Analog Containing A Peptoid Residue at Position P1, PDB code: 4hgc was solved by S.Krzywda, M.Jaskolski, K.Rolka, M.Stawikowski, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.74 / 1.29
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 60.120, 64.140, 70.040, 90.00, 90.00, 90.00
R / Rfree (%) 12.6 / 15.7

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of Bovine Trypsin Complexed with Sfti-1 Analog Containing A Peptoid Residue at Position P1 (pdb code 4hgc). 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 Bovine Trypsin Complexed with Sfti-1 Analog Containing A Peptoid Residue at Position P1, PDB code: 4hgc:

Calcium binding site 1 out of 1 in 4hgc

Go back to Calcium Binding Sites List in 4hgc
Calcium binding site 1 out of 1 in the Crystal Structure of Bovine Trypsin Complexed with Sfti-1 Analog Containing A Peptoid Residue at Position P1


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 Bovine Trypsin Complexed with Sfti-1 Analog Containing A Peptoid Residue at Position P1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca301

b:15.0
occ:1.00
 OE1 A:GLU70 2.3 14.4 1.0
O A:VAL75 2.3 17.4 1.0
OE2 A:GLU80 2.3 16.0 1.0
O A:ASN72 2.3 16.6 1.0
O A:HOH408 2.4 16.7 1.0
O A:HOH419 2.4 15.4 1.0
CD A:GLU80 3.3 15.9 1.0
CD A:GLU70 3.4 13.5 1.0
C A:VAL75 3.5 15.9 1.0
C A:ASN72 3.5 15.8 1.0
CG A:GLU80 3.6 16.1 1.0
OE2 A:GLU70 3.8 14.8 1.0
CA A:VAL76 4.2 18.4 1.0
N A:GLU77 4.2 17.9 1.0
N A:VAL76 4.2 17.3 1.0
N A:VAL75 4.2 18.6 1.0
CA A:ILE73 4.2 16.7 1.0
N A:ILE73 4.3 16.7 1.0
OE1 A:GLU77 4.3 18.6 1.0
O A:HOH420 4.4 17.3 1.0
N A:ASN72 4.4 15.0 1.0
CA A:ASN72 4.5 15.5 1.0
CG A:GLU77 4.5 18.5 1.0
C A:ILE73 4.5 16.3 1.0
CA A:VAL75 4.5 19.0 1.0
OE1 A:GLU80 4.5 16.9 1.0
N A:ASP71 4.6 14.3 1.0
C A:VAL76 4.6 19.9 1.0
CG A:GLU70 4.6 12.6 1.0
O A:HOH495 4.7 25.3 1.0
CA A:GLU70 4.8 12.4 1.0
CB A:ASN72 4.8 16.2 1.0
CB A:GLU77 4.8 19.6 1.0
CB A:GLU70 4.8 12.5 1.0
N A:ASN74 4.8 16.9 1.0
O A:ILE73 4.8 17.9 1.0
CD A:GLU77 4.9 18.6 1.0

Reference:

S.Krzywda, M.Jaskolski, K.Rolka, M.J.Stawikowski. Structure of A Proteolytically Resistant Analogue of (Nlys)(5)Sfti-1 in Complex with Trypsin: Evidence For the Direct Participation of the SER214 Carbonyl Group in Serine Protease-Mediated Proteolysis. Acta Crystallogr.,Sect.D V. 70 668 2014.
ISSN: ISSN 0907-4449
PubMed: 24598736
DOI: 10.1107/S1399004713032252
Page generated: Sat Dec 12 04:50:15 2020

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