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Manganese in PDB 5c47: Crystal Structure of Abbb + Udp-C-Gal (Long Soak) + Di

Enzymatic activity of Crystal Structure of Abbb + Udp-C-Gal (Long Soak) + Di

All present enzymatic activity of Crystal Structure of Abbb + Udp-C-Gal (Long Soak) + Di:
2.4.1.37; 2.4.1.40;

Protein crystallography data

The structure of Crystal Structure of Abbb + Udp-C-Gal (Long Soak) + Di, PDB code: 5c47 was solved by S.Gagnon, P.Meloncelli, R.B.Zheng, O.Haji-Ghassemi, A.R.Johal, S.Borisova, T.L.Lowary, S.V.Evans, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 6.00 / 1.39
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 52.560, 149.350, 79.440, 90.00, 90.00, 90.00
R / Rfree (%) 17.8 / 19.9

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of Abbb + Udp-C-Gal (Long Soak) + Di (pdb code 5c47). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Crystal Structure of Abbb + Udp-C-Gal (Long Soak) + Di, PDB code: 5c47:

Manganese binding site 1 out of 1 in 5c47

Go back to Manganese Binding Sites List in 5c47
Manganese binding site 1 out of 1 in the Crystal Structure of Abbb + Udp-C-Gal (Long Soak) + Di


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of Abbb + Udp-C-Gal (Long Soak) + Di within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn401

b:14.9
occ:1.00
O23 A:URM404 2.1 17.3 1.0
OD2 A:ASP211 2.1 13.5 1.0
O11 A:URM404 2.2 15.4 1.0
OD1 A:ASP213 2.3 13.9 1.0
O A:HOH684 2.3 16.2 1.0
OD2 A:ASP213 2.4 15.3 1.0
CG A:ASP213 2.7 14.5 1.0
CG A:ASP211 3.2 12.8 1.0
P22 A:URM404 3.3 17.7 1.0
P9 A:URM404 3.4 16.5 1.0
O12 A:URM404 3.6 16.6 1.0
CB A:ASP211 3.6 12.8 1.0
O7 A:URM404 3.8 14.7 1.0
O A:HOH521 4.0 25.0 1.0
C45 A:URM404 4.1 19.7 1.0
CB A:ASP213 4.2 13.5 1.0
OD1 A:ASP211 4.3 12.6 1.0
C5 A:URM404 4.3 15.4 1.0
O8 A:URM404 4.4 15.5 1.0
CE A:LYS346 4.4 25.9 1.0
O24 A:URM404 4.5 19.5 1.0
O10 A:URM404 4.5 16.9 1.0
C3 A:URM404 4.6 15.2 1.0
O A:HOH532 4.7 19.6 1.0
O A:ASP213 4.9 13.4 1.0
SD A:MET214 4.9 14.6 1.0
CD A:LYS346 4.9 25.5 1.0
C4 A:URM404 4.9 15.9 1.0
N A:ASP213 5.0 12.3 1.0
CB A:ALA268 5.0 12.0 1.0
CA A:ASP211 5.0 12.0 1.0

Reference:

S.M.Gagnon, P.J.Meloncelli, R.B.Zheng, O.Haji-Ghassemi, A.R.Johal, S.N.Borisova, T.L.Lowary, S.V.Evans. High Resolution Structures of the Human Abo(H) Blood Group Enzymes in Complex with Donor Analogs Reveal That the Enzymes Utilize Multiple Donor Conformations to Bind Substrates in A Stepwise Manner. J.Biol.Chem. V. 290 27040 2015.
ISSN: ESSN 1083-351X
PubMed: 26374898
DOI: 10.1074/JBC.M115.682401
Page generated: Tue Dec 15 04:36:22 2020

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