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Manganese in PDB 2d7r: Crystal Structure of Pp-Galnac-T10 Complexed with Galnac-Ser on Lectin Domain

Enzymatic activity of Crystal Structure of Pp-Galnac-T10 Complexed with Galnac-Ser on Lectin Domain

All present enzymatic activity of Crystal Structure of Pp-Galnac-T10 Complexed with Galnac-Ser on Lectin Domain:
2.4.1.41;

Protein crystallography data

The structure of Crystal Structure of Pp-Galnac-T10 Complexed with Galnac-Ser on Lectin Domain, PDB code: 2d7r 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 / 2.80
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 80.195, 132.812, 138.953, 90.00, 90.00, 90.00
R / Rfree (%) 22.9 / 29.8

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of Pp-Galnac-T10 Complexed with Galnac-Ser on Lectin Domain (pdb code 2d7r). 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 Complexed with Galnac-Ser on Lectin Domain, PDB code: 2d7r:

Manganese binding site 1 out of 1 in 2d7r

Go back to Manganese Binding Sites List in 2d7r
Manganese binding site 1 out of 1 in the Crystal Structure of Pp-Galnac-T10 Complexed with Galnac-Ser on Lectin Domain


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 Complexed with Galnac-Ser on Lectin Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn706

b:24.3
occ:1.00
O A:HOH711 2.1 24.7 1.0
OD2 A:ASP237 2.1 27.4 1.0
O1B A:UDP705 2.2 56.2 1.0
NE2 A:HIS370 2.3 22.0 1.0
O1A A:UDP705 2.3 59.4 1.0
NE2 A:HIS239 2.3 37.5 1.0
CE1 A:HIS370 3.1 24.2 1.0
CG A:ASP237 3.2 32.1 1.0
CD2 A:HIS239 3.2 36.8 1.0
PB A:UDP705 3.2 52.7 1.0
CE1 A:HIS239 3.3 37.0 1.0
CD2 A:HIS370 3.4 23.2 1.0
PA A:UDP705 3.5 57.6 1.0
O2B A:UDP705 3.5 55.9 1.0
O3A A:UDP705 3.7 56.5 1.0
CB A:ASP237 3.8 32.1 1.0
OD1 A:ASP237 4.2 35.0 1.0
C5' A:UDP705 4.3 54.5 1.0
ND1 A:HIS370 4.3 23.1 1.0
ND1 A:HIS239 4.4 36.4 1.0
CG A:HIS239 4.4 36.2 1.0
O A:ILE371 4.4 24.9 1.0
O5' A:UDP705 4.4 57.8 1.0
CG A:HIS370 4.5 26.3 1.0
O3B A:UDP705 4.6 53.9 1.0
O2A A:UDP705 4.6 55.7 1.0
O3 A:NGA702 4.6 47.2 1.0
C3' A:UDP705 4.7 53.4 1.0
N2 A:NGA702 4.7 45.7 1.0
NE A:ARG373 4.9 24.1 1.0
C8 A:NGA702 4.9 44.8 1.0
NH2 A:ARG373 4.9 25.4 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 13:44:42 2024

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