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Cobalt in PDB 5nrb: A Native Ternary Complex of Alpha-1,3-Galactosyltransferase (A-3GALT) Supports A Conserved Reaction Mechanism For Retaining Glycosyltransferases - Alpha-3GALT in Complex with CO2+, Udp-Gal and Lactose - A3GALT-CO2+-Udp-Gal-Lat-1

Enzymatic activity of A Native Ternary Complex of Alpha-1,3-Galactosyltransferase (A-3GALT) Supports A Conserved Reaction Mechanism For Retaining Glycosyltransferases - Alpha-3GALT in Complex with CO2+, Udp-Gal and Lactose - A3GALT-CO2+-Udp-Gal-Lat-1

All present enzymatic activity of A Native Ternary Complex of Alpha-1,3-Galactosyltransferase (A-3GALT) Supports A Conserved Reaction Mechanism For Retaining Glycosyltransferases - Alpha-3GALT in Complex with CO2+, Udp-Gal and Lactose - A3GALT-CO2+-Udp-Gal-Lat-1:
2.4.1.87;

Protein crystallography data

The structure of A Native Ternary Complex of Alpha-1,3-Galactosyltransferase (A-3GALT) Supports A Conserved Reaction Mechanism For Retaining Glycosyltransferases - Alpha-3GALT in Complex with CO2+, Udp-Gal and Lactose - A3GALT-CO2+-Udp-Gal-Lat-1, PDB code: 5nrb was solved by D.Albesa-Jove, A.Marina, M.A.Sainz-Polo, M.E.Guerin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 58.56 / 2.24
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 132.963, 65.646, 82.654, 90.00, 102.92, 90.00
R / Rfree (%) 19.9 / 24.6

Cobalt Binding Sites:

The binding sites of Cobalt atom in the A Native Ternary Complex of Alpha-1,3-Galactosyltransferase (A-3GALT) Supports A Conserved Reaction Mechanism For Retaining Glycosyltransferases - Alpha-3GALT in Complex with CO2+, Udp-Gal and Lactose - A3GALT-CO2+-Udp-Gal-Lat-1 (pdb code 5nrb). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total 2 binding sites of Cobalt where determined in the A Native Ternary Complex of Alpha-1,3-Galactosyltransferase (A-3GALT) Supports A Conserved Reaction Mechanism For Retaining Glycosyltransferases - Alpha-3GALT in Complex with CO2+, Udp-Gal and Lactose - A3GALT-CO2+-Udp-Gal-Lat-1, PDB code: 5nrb:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 in 5nrb

Go back to Cobalt Binding Sites List in 5nrb
Cobalt binding site 1 out of 2 in the A Native Ternary Complex of Alpha-1,3-Galactosyltransferase (A-3GALT) Supports A Conserved Reaction Mechanism For Retaining Glycosyltransferases - Alpha-3GALT in Complex with CO2+, Udp-Gal and Lactose - A3GALT-CO2+-Udp-Gal-Lat-1


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of A Native Ternary Complex of Alpha-1,3-Galactosyltransferase (A-3GALT) Supports A Conserved Reaction Mechanism For Retaining Glycosyltransferases - Alpha-3GALT in Complex with CO2+, Udp-Gal and Lactose - A3GALT-CO2+-Udp-Gal-Lat-1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Co402

b:52.3
occ:0.51
O A:HOH505 2.1 53.1 0.5
O1B A:GDU403 2.2 54.8 0.5
O1A A:GDU403 2.3 52.7 0.5
OD2 A:ASP225 2.4 41.8 1.0
OD1 A:ASP227 2.7 51.2 1.0
HZ1 A:LYS359 2.7 91.5 1.0
HZ3 A:LYS359 2.8 91.5 1.0
OD2 A:ASP227 3.0 58.0 1.0
PB A:GDU403 3.0 45.7 0.5
HO2A A:GDU403 3.1 55.8 0.5
O3B A:GDU403 3.1 53.8 0.5
H5'1 A:GDU403 3.2 51.3 0.5
NZ A:LYS359 3.2 76.2 1.0
CG A:ASP227 3.2 48.5 1.0
HB3 A:ASP225 3.3 50.1 1.0
PA A:GDU403 3.3 48.8 0.5
O2' A:GDU403 3.4 46.5 0.5
O3A A:GDU403 3.4 48.2 0.5
CG A:ASP225 3.4 32.5 1.0
O3D A:GDU403 3.7 37.9 0.5
CB A:ASP225 3.7 41.7 1.0
HZ2 A:LYS359 3.8 91.5 1.0
HB2 A:ASP225 3.9 50.1 1.0
O A:HOH507 3.9 65.8 1.0
C1' A:GDU403 4.0 55.5 0.5
HE2 A:LYS359 4.1 90.9 1.0
HB2 A:ALA282 4.1 24.7 1.0
C5D A:GDU403 4.1 42.7 0.5
H1' A:GDU403 4.2 66.6 0.5
H3' A:GDU403 4.2 40.5 0.5
C2' A:GDU403 4.3 41.4 0.5
CE A:LYS359 4.3 75.7 1.0
O5D A:GDU403 4.3 44.8 0.5
HE2 A:HIS280 4.4 48.1 1.0
O2B A:GDU403 4.4 53.0 0.5
H3D A:GDU403 4.4 52.4 0.5
O2A A:GDU403 4.5 47.8 0.5
C3D A:GDU403 4.5 43.6 0.5
OD1 A:ASP225 4.5 36.9 1.0
HB1 A:ALA282 4.7 24.7 1.0
C4D A:GDU403 4.7 45.6 0.5
HG2 A:LYS359 4.7 0.1 1.0
CB A:ASP227 4.7 41.8 1.0
HG3 A:LYS359 4.7 0.1 1.0
H A:ASP227 4.8 29.0 1.0
CB A:ALA282 4.8 20.6 1.0
HE3 A:LYS359 4.8 90.9 1.0
C3' A:GDU403 4.8 33.8 0.5
O A:ASP227 4.9 37.6 1.0
H4D A:GDU403 4.9 54.7 0.5
H5'2 A:GDU403 4.9 51.3 0.5
HOA2 A:GDU403 4.9 57.4 0.5

Cobalt binding site 2 out of 2 in 5nrb

Go back to Cobalt Binding Sites List in 5nrb
Cobalt binding site 2 out of 2 in the A Native Ternary Complex of Alpha-1,3-Galactosyltransferase (A-3GALT) Supports A Conserved Reaction Mechanism For Retaining Glycosyltransferases - Alpha-3GALT in Complex with CO2+, Udp-Gal and Lactose - A3GALT-CO2+-Udp-Gal-Lat-1


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 2 of A Native Ternary Complex of Alpha-1,3-Galactosyltransferase (A-3GALT) Supports A Conserved Reaction Mechanism For Retaining Glycosyltransferases - Alpha-3GALT in Complex with CO2+, Udp-Gal and Lactose - A3GALT-CO2+-Udp-Gal-Lat-1 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Co401

b:49.8
occ:0.59
O B:HOH528 2.2 45.9 1.0
O1A B:GDU402 2.3 44.6 0.6
OD2 B:ASP227 2.3 52.2 1.0
O1B B:GDU402 2.4 49.8 0.6
O B:HOH574 2.8 51.8 0.6
CG B:ASP227 3.1 44.9 1.0
OD1 B:ASP227 3.1 44.8 1.0
PB B:GDU402 3.2 54.3 0.6
PA B:GDU402 3.3 43.5 0.6
O3A B:GDU402 3.4 40.2 0.6
O3B B:GDU402 3.6 53.2 0.6
H5'1 B:GDU402 4.0 53.7 0.6
O2A B:GDU402 4.1 53.0 0.6
HOA2 B:GDU402 4.3 63.7 0.6
HO2A B:GDU402 4.4 46.2 0.6
OD2 B:ASP225 4.5 46.9 1.0
CB B:ASP227 4.5 36.6 1.0
HB3 B:ASP225 4.5 46.2 1.0
O5D B:GDU402 4.6 40.4 0.6
HB2 B:ASP227 4.6 43.9 1.0
O3D B:GDU402 4.7 40.9 0.6
O2B B:GDU402 4.7 52.0 0.6
HH B:TYR139 4.7 80.0 1.0
HE1 B:TYR139 4.7 78.3 1.0
H3D B:GDU402 4.8 62.1 0.6
C5D B:GDU402 4.8 44.7 0.6
HB3 B:ASP227 4.8 43.9 1.0
C1' B:GDU402 4.8 45.1 0.6
O2' B:GDU402 5.0 38.5 0.6
H1' B:GDU402 5.0 54.2 0.6

Reference:

D.Albesa-Jove, M.A.Sainz-Polo, A.Marina, M.E.Guerin. Structural Snapshots of Alpha-1,3-Galactosyltransferase with Native Substrates: Insight Into the Catalytic Mechanism of Retaining Glycosyltransferases. Angew. Chem. Int. Ed. Engl. V. 56 14853 2017.
ISSN: ESSN 1521-3773
PubMed: 28960760
DOI: 10.1002/ANIE.201707922
Page generated: Tue Jul 30 18:11:31 2024

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