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Manganese in PDB 2d7i: Crystal Structure of Pp-Galnac-T10 with Udp, Galnac and MN2+

Enzymatic activity of Crystal Structure of Pp-Galnac-T10 with Udp, Galnac and MN2+

All present enzymatic activity of Crystal Structure of Pp-Galnac-T10 with Udp, Galnac and MN2+:
2.4.1.41;

Protein crystallography data

The structure of Crystal Structure of Pp-Galnac-T10 with Udp, Galnac and MN2+, PDB code: 2d7i was solved by T.Kubota, T.Shiba, S.Sugioka, R.Kato, S.Wakatsuki, H.Narimatsu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.00 / 2.50
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 79.855, 133.375, 138.713, 90.00, 90.00, 90.00
R / Rfree (%) 21.5 / 26.7

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of Pp-Galnac-T10 with Udp, Galnac and MN2+ (pdb code 2d7i). 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 Pp-Galnac-T10 with Udp, Galnac and MN2+, PDB code: 2d7i:

Manganese binding site 1 out of 1 in 2d7i

Go back to Manganese Binding Sites List in 2d7i
Manganese binding site 1 out of 1 in the Crystal Structure of Pp-Galnac-T10 with Udp, Galnac and MN2+


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 Pp-Galnac-T10 with Udp, Galnac and MN2+ within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn706

b:30.9
occ:1.00
O A:HOH711 2.1 33.1 1.0
O1B A:UDP705 2.1 35.6 1.0
OD2 A:ASP237 2.2 38.0 1.0
NE2 A:HIS239 2.2 31.9 1.0
NE2 A:HIS370 2.3 31.6 1.0
O1A A:UDP705 2.3 39.1 1.0
CE1 A:HIS370 3.1 31.6 1.0
CD2 A:HIS239 3.2 30.7 1.0
PB A:UDP705 3.2 37.1 1.0
CE1 A:HIS239 3.3 32.6 1.0
CG A:ASP237 3.3 38.2 1.0
CD2 A:HIS370 3.5 31.8 1.0
O2B A:UDP705 3.5 37.3 1.0
PA A:UDP705 3.5 39.2 1.0
O3A A:UDP705 3.6 37.5 1.0
CB A:ASP237 3.8 35.5 1.0
C5' A:UDP705 4.3 38.6 1.0
ND1 A:HIS370 4.3 31.1 1.0
CG A:HIS239 4.3 28.5 1.0
ND1 A:HIS239 4.4 30.8 1.0
OD1 A:ASP237 4.4 41.2 1.0
O A:ILE371 4.4 31.4 1.0
O5' A:UDP705 4.4 39.0 1.0
O3B A:UDP705 4.5 36.2 1.0
CG A:HIS370 4.5 32.4 1.0
N2 A:NGA702 4.5 58.8 1.0
O3 A:NGA702 4.5 58.2 1.0
O2A A:UDP705 4.6 38.8 1.0
C3' A:UDP705 4.8 37.1 1.0
O A:HOH713 4.8 36.3 1.0
C3 A:NGA702 4.9 58.6 1.0
C8 A:NGA702 4.9 57.7 1.0

Reference:

T.Kubota, T.Shiba, S.Sugioka, S.Furukawa, H.Sawaki, R.Kato, S.Wakatsuki, H.Narimatsu. Structural Basis of Carbohydrate Transfer Activity By Human Udp-Galnac: Polypeptide Alpha-N-Acetylgalactosaminyltransferase (Pp-Galnac-T10) J.Mol.Biol. V. 359 708 2006.
ISSN: ISSN 0022-2836
PubMed: 16650853
DOI: 10.1016/J.JMB.2006.03.061
Page generated: Sat Oct 5 13:44:09 2024

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