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Calcium in PDB 1slv: Rat Anionic N143H, E151H Trypsin Complexed to A86H Ecotin; Copper- Bound

Enzymatic activity of Rat Anionic N143H, E151H Trypsin Complexed to A86H Ecotin; Copper- Bound

All present enzymatic activity of Rat Anionic N143H, E151H Trypsin Complexed to A86H Ecotin; Copper- Bound:
3.4.21.4;

Protein crystallography data

The structure of Rat Anionic N143H, E151H Trypsin Complexed to A86H Ecotin; Copper- Bound, PDB code: 1slv was solved by L.S.Brinen, 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 C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 86.350, 56.590, 81.400, 90.00, 92.99, 90.00
R / Rfree (%) 19.5 / 27.8

Other elements in 1slv:

The structure of Rat Anionic N143H, E151H Trypsin Complexed to A86H Ecotin; Copper- Bound also contains other interesting chemical elements:

Copper (Cu) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the Rat Anionic N143H, E151H Trypsin Complexed to A86H Ecotin; Copper- Bound (pdb code 1slv). 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 Rat Anionic N143H, E151H Trypsin Complexed to A86H Ecotin; Copper- Bound, PDB code: 1slv:

Calcium binding site 1 out of 1 in 1slv

Go back to Calcium Binding Sites List in 1slv
Calcium binding site 1 out of 1 in the Rat Anionic N143H, E151H Trypsin Complexed to A86H Ecotin; Copper- Bound


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Rat Anionic N143H, E151H Trypsin Complexed to A86H Ecotin; Copper- Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca246

b:32.8
occ:1.00
O B:ACT247 1.6 46.0 1.0
O B:VAL75 1.9 38.0 1.0
O B:ASN72 2.0 30.2 1.0
C B:ACT247 2.2 44.7 1.0
OXT B:ACT247 2.2 42.4 1.0
OE1 B:GLU70 2.5 22.5 1.0
OE2 B:GLU77 2.6 41.7 1.0
O B:HOH276 3.1 51.8 1.0
C B:VAL75 3.1 36.7 1.0
C B:ASN72 3.2 30.1 1.0
CD B:GLU77 3.4 44.0 1.0
CD B:GLU70 3.6 20.5 1.0
CH3 B:ACT247 3.7 42.5 1.0
N B:LEU76 3.9 37.8 1.0
OE2 B:GLU70 4.0 23.1 1.0
CA B:LEU76 4.0 38.7 1.0
N B:VAL75 4.1 37.4 1.0
N B:ILE73 4.1 31.6 1.0
CG B:GLU77 4.2 41.4 1.0
CA B:VAL75 4.2 36.9 1.0
OE1 B:GLU77 4.2 44.9 1.0
CA B:ASN72 4.2 28.4 1.0
N B:ASN72 4.2 26.2 1.0
CA B:ILE73 4.3 31.9 1.0
CB B:ASN72 4.3 29.7 1.0
C B:ILE73 4.3 33.7 1.0
N B:GLU77 4.4 39.9 1.0
C B:LEU76 4.5 39.8 1.0
O B:ILE73 4.5 34.5 1.0
CG2 B:VAL75 4.6 38.4 1.0
N B:ASN74 4.7 34.6 1.0
N B:HIS71 4.8 22.9 1.0
CG B:GLU70 4.8 19.5 1.0
OD1 B:ASN72 4.9 33.8 1.0
C B:ASN74 4.9 37.8 1.0
CA B:GLU70 4.9 20.4 1.0

Reference:

L.S.Brinen, W.S.Willett, C.S.Craik, R.J.Fletterick. X-Ray Structures of A Designed Binding Site in Trypsin Show Metal-Dependent Geometry. Biochemistry V. 35 5999 1996.
ISSN: ISSN 0006-2960
PubMed: 8634241
DOI: 10.1021/BI9530200
Page generated: Sat Dec 12 03:19:34 2020

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