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Copper in PDB 1and: Anionic Trypsin Mutant with Arg 96 Replaced By His

Enzymatic activity of Anionic Trypsin Mutant with Arg 96 Replaced By His

All present enzymatic activity of Anionic Trypsin Mutant with Arg 96 Replaced By His:
3.4.21.4;

Protein crystallography data

The structure of Anionic Trypsin Mutant with Arg 96 Replaced By His, PDB code: 1and was solved by R.J.Fletterick, M.E.Mcgrath, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 7.00 / 2.30
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 (%) 16.1 / n/a

Copper Binding Sites:

The binding sites of Copper atom in the Anionic Trypsin Mutant with Arg 96 Replaced By His (pdb code 1and). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total only one binding site of Copper was determined in the Anionic Trypsin Mutant with Arg 96 Replaced By His, PDB code: 1and:

Copper binding site 1 out of 1 in 1and

Go back to Copper Binding Sites List in 1and
Copper binding site 1 out of 1 in the Anionic Trypsin Mutant with Arg 96 Replaced By His


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Anionic Trypsin Mutant with Arg 96 Replaced By His within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu246

b:16.4
occ:1.00
NE2 A:HIS96 2.2 16.7 1.0
NE2 A:HIS57 2.2 17.4 1.0
CE1 A:HIS96 3.0 33.6 1.0
CD2 A:HIS57 3.2 18.2 1.0
CE1 A:HIS57 3.2 17.4 1.0
CD2 A:HIS96 3.2 29.0 1.0
ND1 A:HIS96 4.2 35.8 1.0
CG A:HIS57 4.3 15.4 1.0
CG A:HIS96 4.3 27.9 1.0
ND1 A:HIS57 4.3 16.2 1.0

Reference:

M.E.Mcgrath, B.L.Haymore, N.L.Summers, C.S.Craik, R.J.Fletterick. Structure of An Engineered, Metal-Actuated Switch in Trypsin. Biochemistry V. 32 1914 1993.
ISSN: ISSN 0006-2960
PubMed: 8448149
DOI: 10.1021/BI00059A005
Page generated: Sun Dec 13 10:57:40 2020

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