Atomistry » Calcium » PDB 5mfd-5mnl » 5mi7
Atomistry »
  Calcium »
    PDB 5mfd-5mnl »
      5mi7 »

Calcium in PDB 5mi7: BTGH84 Mutant with Covalent Modification By MA4 in Complex with Pugnac

Enzymatic activity of BTGH84 Mutant with Covalent Modification By MA4 in Complex with Pugnac

All present enzymatic activity of BTGH84 Mutant with Covalent Modification By MA4 in Complex with Pugnac:
3.2.1.169; 3.2.1.52;

Protein crystallography data

The structure of BTGH84 Mutant with Covalent Modification By MA4 in Complex with Pugnac, PDB code: 5mi7 was solved by J.F.Darby, G.J.Davies, R.E.Hubbard, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 100.62 / 2.10
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 195.193, 51.823, 108.234, 90.00, 111.61, 90.00
R / Rfree (%) 21.3 / 24.9

Calcium Binding Sites:

The binding sites of Calcium atom in the BTGH84 Mutant with Covalent Modification By MA4 in Complex with Pugnac (pdb code 5mi7). 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 BTGH84 Mutant with Covalent Modification By MA4 in Complex with Pugnac, PDB code: 5mi7:

Calcium binding site 1 out of 1 in 5mi7

Go back to Calcium Binding Sites List in 5mi7
Calcium binding site 1 out of 1 in the BTGH84 Mutant with Covalent Modification By MA4 in Complex with Pugnac


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of BTGH84 Mutant with Covalent Modification By MA4 in Complex with Pugnac within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca803

b:40.5
occ:1.00
O A:GLU32 2.3 40.0 1.0
O A:HOH1014 2.4 31.7 1.0
OE1 A:GLU61 2.4 42.5 1.0
O A:HOH1032 2.4 39.6 1.0
OD2 A:ASP64 2.5 34.4 1.0
O A:HOH916 2.5 46.1 1.0
OD1 A:ASP64 2.5 45.9 1.0
CG A:ASP64 2.8 38.3 1.0
HB2 A:GLU61 3.2 56.3 1.0
C A:GLU32 3.4 40.5 1.0
HA A:ALA33 3.5 43.0 1.0
CD A:GLU61 3.6 46.8 1.0
H A:GLU61 3.7 40.7 1.0
HB3 A:GLU32 3.9 75.3 1.0
CB A:GLU61 4.1 46.9 1.0
CA A:ALA33 4.3 35.8 1.0
N A:ALA33 4.3 39.0 1.0
CG A:GLU61 4.3 43.8 1.0
HA A:GLU32 4.3 64.5 1.0
CB A:ASP64 4.3 42.7 1.0
CA A:GLU32 4.4 53.7 1.0
HG2 A:GLU61 4.4 52.6 1.0
HG2 A:GLU97 4.5 75.0 1.0
N A:GLU61 4.5 33.9 1.0
CB A:GLU32 4.5 62.8 1.0
OE2 A:GLU61 4.6 40.0 1.0
HB3 A:ASP64 4.7 51.2 1.0
HB2 A:GLU32 4.7 75.3 1.0
C A:ALA33 4.7 33.9 1.0
HB3 A:GLU61 4.8 56.3 1.0
HB2 A:ASP64 4.8 51.2 1.0
OE2 A:GLU97 4.8 73.1 1.0
H A:ASN34 4.9 45.1 1.0
CA A:GLU61 4.9 41.4 1.0
H A:ASP64 5.0 58.4 1.0
HA2 A:GLY60 5.0 42.4 1.0

Reference:

J.F.Darby, M.Atobe, J.D.Firth, P.Bond, G.J.Davies, P.O'brien, R.E.Hubbard. Increase of Enzyme Activity Through Specific Covalent Modification with Fragments. Chem Sci V. 8 7772 2017.
ISSN: ISSN 2041-6520
PubMed: 29163914
DOI: 10.1039/C7SC01966A
Page generated: Sat Dec 12 05:37:53 2020

Last articles

Zn in 7VD8
Zn in 7V1R
Zn in 7V1Q
Zn in 7VPF
Zn in 7T85
Zn in 7T5F
Zn in 7NF9
Zn in 7M4M
Zn in 7M4O
Zn in 7M4N
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy