Atomistry » Calcium » PDB 1tkj-1ttx » 1trm
Atomistry »
  Calcium »
    PDB 1tkj-1ttx »
      1trm »

Calcium in PDB 1trm: The Three-Dimensional Structure of ASN102 Mutant of Trypsin. Role of ASP102 in Serine Protease Catalysis

Enzymatic activity of The Three-Dimensional Structure of ASN102 Mutant of Trypsin. Role of ASP102 in Serine Protease Catalysis

All present enzymatic activity of The Three-Dimensional Structure of ASN102 Mutant of Trypsin. Role of ASP102 in Serine Protease Catalysis:
3.4.21.4;

Protein crystallography data

The structure of The Three-Dimensional Structure of ASN102 Mutant of Trypsin. Role of ASP102 in Serine Protease Catalysis, PDB code: 1trm was solved by S.Sprang, T.Standing, R.J.Fletterick, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 6.00 / 2.30
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 40.400, 92.000, 127.300, 90.00, 90.00, 90.00
R / Rfree (%) n/a / n/a

Calcium Binding Sites:

The binding sites of Calcium atom in the The Three-Dimensional Structure of ASN102 Mutant of Trypsin. Role of ASP102 in Serine Protease Catalysis (pdb code 1trm). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the The Three-Dimensional Structure of ASN102 Mutant of Trypsin. Role of ASP102 in Serine Protease Catalysis, PDB code: 1trm:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 1trm

Go back to Calcium Binding Sites List in 1trm
Calcium binding site 1 out of 2 in the The Three-Dimensional Structure of ASN102 Mutant of Trypsin. Role of ASP102 in Serine Protease Catalysis


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of The Three-Dimensional Structure of ASN102 Mutant of Trypsin. Role of ASP102 in Serine Protease Catalysis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca247

b:13.9
occ:1.00
OE1 A:GLU77 2.0 13.4 1.0
OE1 A:GLU70 2.2 14.3 1.0
O A:ASN72 2.4 18.1 1.0
O A:HOH271 2.4 5.3 1.0
O A:VAL75 2.4 21.1 1.0
OE2 A:GLU80 2.5 25.9 1.0
CD A:GLU77 2.9 29.6 1.0
CD A:GLU70 3.2 14.2 1.0
C A:VAL75 3.3 20.0 1.0
CD A:GLU80 3.3 24.4 1.0
CG A:GLU77 3.5 31.0 1.0
C A:ASN72 3.5 15.5 1.0
CG A:GLU80 3.8 21.5 1.0
OE2 A:GLU70 3.8 19.2 1.0
N A:GLU77 3.9 20.7 1.0
N A:LEU76 4.0 22.0 1.0
CA A:LEU76 4.0 20.6 1.0
OE1 A:GLU80 4.1 31.0 1.0
OE2 A:GLU77 4.2 27.4 1.0
N A:VAL75 4.3 20.5 1.0
C A:LEU76 4.3 16.3 1.0
CA A:ILE73 4.4 10.5 1.0
CG A:GLU70 4.4 14.3 1.0
CA A:VAL75 4.4 17.4 1.0
N A:ILE73 4.4 8.5 1.0
C A:ILE73 4.4 17.0 1.0
N A:ASN72 4.5 11.7 1.0
CA A:ASN72 4.5 14.7 1.0
CB A:GLU77 4.5 19.1 1.0
O A:ILE73 4.7 17.7 1.0
CB A:ASN72 4.7 11.0 1.0
N A:HIS71 4.8 10.7 1.0
CA A:GLU77 4.9 23.2 1.0
CB A:GLU70 4.9 18.1 1.0
N A:ASN74 4.9 18.9 1.0
CD2 A:LEU76 4.9 27.1 1.0
O A:HOH254 5.0 17.3 1.0

Calcium binding site 2 out of 2 in 1trm

Go back to Calcium Binding Sites List in 1trm
Calcium binding site 2 out of 2 in the The Three-Dimensional Structure of ASN102 Mutant of Trypsin. Role of ASP102 in Serine Protease Catalysis


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of The Three-Dimensional Structure of ASN102 Mutant of Trypsin. Role of ASP102 in Serine Protease Catalysis within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca247

b:17.5
occ:1.00
OE1 B:GLU77 1.8 32.4 1.0
O B:HOH272 2.0 2.4 1.0
O B:VAL75 2.3 28.8 1.0
O B:ASN72 2.3 15.6 1.0
OE1 B:GLU70 2.3 13.9 1.0
OE2 B:GLU80 2.5 19.7 1.0
CD B:GLU77 2.7 38.4 1.0
CD B:GLU70 3.3 8.3 1.0
C B:ASN72 3.4 18.4 1.0
C B:VAL75 3.4 21.7 1.0
CD B:GLU80 3.5 17.2 1.0
CG B:GLU77 3.5 36.9 1.0
OE2 B:GLU70 3.7 16.0 1.0
OE2 B:GLU77 3.8 34.4 1.0
CG B:GLU80 3.8 8.2 1.0
N B:ASN72 4.1 18.2 1.0
N B:LEU76 4.2 21.9 1.0
CA B:ASN72 4.2 17.0 1.0
N B:GLU77 4.2 20.8 1.0
N B:VAL75 4.3 17.7 1.0
CA B:LEU76 4.3 18.1 1.0
N B:ILE73 4.4 14.3 1.0
OE1 B:GLU80 4.4 16.5 1.0
CB B:ASN72 4.5 16.1 1.0
C B:ILE73 4.5 22.5 1.0
N B:HIS71 4.5 6.3 1.0
C B:LEU76 4.5 16.3 1.0
CA B:VAL75 4.5 18.9 1.0
CB B:GLU77 4.6 21.8 1.0
CA B:ILE73 4.6 17.4 1.0
CG B:GLU70 4.6 13.0 1.0
N B:ASN74 4.7 20.9 1.0
O B:ILE73 4.8 22.9 1.0
CA B:GLU70 4.8 10.8 1.0
CB B:GLU70 4.9 14.9 1.0
C B:HIS71 5.0 19.8 1.0

Reference:

S.Sprang, T.Standing, R.J.Fletterick, R.M.Stroud, J.Finer-Moore, N.H.Xuong, R.Hamlin, W.J.Rutter, C.S.Craik. The Three-Dimensional Structure of ASN102 Mutant of Trypsin: Role of ASP102 in Serine Protease Catalysis. Science V. 237 905 1987.
ISSN: ISSN 0036-8075
PubMed: 3112942
Page generated: Thu Jul 11 23:11:43 2024

Last articles

Zn in 9MJ5
Zn in 9HNW
Zn in 9G0L
Zn in 9FNE
Zn in 9DZN
Zn in 9E0I
Zn in 9D32
Zn in 9DAK
Zn in 8ZXC
Zn in 8ZUF
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy