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Calcium in PDB 4aiu: A Complex Structure of BTGH84

Enzymatic activity of A Complex Structure of BTGH84

All present enzymatic activity of A Complex Structure of BTGH84:
3.2.1.169; 3.2.1.52;

Protein crystallography data

The structure of A Complex Structure of BTGH84, PDB code: 4aiu was solved by Y.He, G.J.Davies, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.71 / 2.25
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 185.550, 52.030, 85.900, 90.00, 99.79, 90.00
R / Rfree (%) 19.538 / 24.672

Calcium Binding Sites:

The binding sites of Calcium atom in the A Complex Structure of BTGH84 (pdb code 4aiu). 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 A Complex Structure of BTGH84, PDB code: 4aiu:

Calcium binding site 1 out of 1 in 4aiu

Go back to Calcium Binding Sites List in 4aiu
Calcium binding site 1 out of 1 in the A Complex Structure of BTGH84


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of A Complex Structure of BTGH84 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca1590

b:70.0
occ:1.00
O A:GLU32 2.5 42.8 1.0
OE1 A:GLU61 2.5 42.9 1.0
O A:HOH2006 2.6 57.4 1.0
OD2 A:ASP64 2.7 47.4 1.0
OD1 A:ASP64 2.8 49.9 1.0
CG A:ASP64 3.1 50.1 1.0
CD A:GLU61 3.6 43.1 1.0
C A:GLU32 3.7 46.5 1.0
CB A:GLU61 4.0 38.3 1.0
CA A:ALA33 4.1 45.4 1.0
CG A:GLU61 4.2 41.2 1.0
N A:ALA33 4.4 45.3 1.0
N A:GLU61 4.5 36.5 1.0
OE2 A:GLU61 4.5 40.2 1.0
CB A:ASP64 4.6 49.3 1.0
C A:ALA33 4.7 43.0 1.0
CA A:GLU32 4.7 51.9 1.0
CB A:GLU32 4.8 59.8 1.0
CA A:GLU61 4.8 40.7 1.0
N A:ASN34 4.9 44.7 1.0
OE1 A:GLU32 4.9 79.2 1.0

Reference:

M.S.Macauley, J.Chan, W.F.Zandberg, Y.He, G.E.Whitworth, K.A.Stubbs, S.A.Yuzwa, A.J.Bennet, A.Varki, G.J.Davies, D.J.Vocadlo. Metabolism of Vertebrate Amino Sugars with N-Glycolyl Groups: Intracellular Beta-O-Linked N-Glycolylglucosamine (Glcngc), Udp-Glcngc, and the Biochemical and Structural Rationale For the Substrate Tolerance of Beta-O-Linked Beta-N-Acetylglucosaminidase. J.Biol.Chem. V. 287 28882 2012.
ISSN: ISSN 0021-9258
PubMed: 22692202
DOI: 10.1074/JBC.M112.363721
Page generated: Sat Dec 12 04:38:58 2020

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