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Calcium in PDB 2trm: 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: 2trm was solved by R.M.Stroud, J.Finer-Moore, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 7.00 / 2.80
Space group I 2 3
Cell size a, b, c (Å), α, β, γ (°) 124.380, 124.380, 124.380, 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 2trm). 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 The Three-Dimensional Structure of ASN102 Mutant of Trypsin. Role of ASP102 in Serine Protease Catalysis, PDB code: 2trm:

Calcium binding site 1 out of 1 in 2trm

Go back to Calcium Binding Sites List in 2trm
Calcium binding site 1 out of 1 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:33.5
occ:1.00
 OE2 A:GLU80 1.9 12.0 1.0
OE1 A:GLU70 2.0 6.0 1.0
O A:VAL75 2.7 5.0 1.0
O A:ASN72 2.7 11.4 1.0
OE1 A:GLU77 2.8 6.8 1.0
CD A:GLU70 2.9 5.7 1.0
CD A:GLU80 3.2 6.0 1.0
OE2 A:GLU70 3.3 5.1 1.0
C A:VAL75 3.5 5.8 1.0
CD A:GLU77 3.7 9.0 1.0
CG A:GLU80 3.8 7.5 1.0
C A:ASN72 3.9 9.9 1.0
CA A:LEU76 4.0 7.5 1.0
N A:GLU77 4.0 7.3 1.0
OE1 A:GLU80 4.0 9.3 1.0
N A:LEU76 4.1 6.9 1.0
CG A:GLU77 4.2 9.1 1.0
CD2 A:LEU76 4.2 8.6 1.0
CG A:GLU70 4.3 5.4 1.0
N A:VAL75 4.3 7.0 1.0
C A:LEU76 4.4 7.5 1.0
CA A:VAL75 4.6 6.0 1.0
C A:ILE73 4.6 9.5 1.0
CA A:ILE73 4.6 9.1 1.0
O A:ILE73 4.7 9.4 1.0
CB A:GLU77 4.7 9.1 1.0
N A:ILE73 4.8 10.3 1.0
OE2 A:GLU77 4.8 6.5 1.0
N A:ASN72 4.8 8.3 1.0
CA A:ASN72 4.9 9.6 1.0
CB A:GLU70 4.9 4.2 1.0
CA A:GLU70 4.9 5.3 1.0
CB A:ASN72 4.9 7.2 1.0
CA A:GLU77 5.0 7.8 1.0
N A:ASN74 5.0 9.2 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: Sat Dec 12 03:52:49 2020

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