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Lanthanum in PDB 5kij: Crystal Structure of the Class I Human Endoplasmic Reticulum 1,2- Alpha-Mannosidase and MAN9GLCNAC2-Pa Complex

Enzymatic activity of Crystal Structure of the Class I Human Endoplasmic Reticulum 1,2- Alpha-Mannosidase and MAN9GLCNAC2-Pa Complex

All present enzymatic activity of Crystal Structure of the Class I Human Endoplasmic Reticulum 1,2- Alpha-Mannosidase and MAN9GLCNAC2-Pa Complex:
3.2.1.113;

Protein crystallography data

The structure of Crystal Structure of the Class I Human Endoplasmic Reticulum 1,2- Alpha-Mannosidase and MAN9GLCNAC2-Pa Complex, PDB code: 5kij was solved by K.Karaveg, Y.Xiang, K.W.Moremen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 27.08 / 1.65
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 50.625, 53.830, 56.118, 89.65, 63.60, 62.70
R / Rfree (%) 18.3 / 22.2

Lanthanum Binding Sites:

The binding sites of Lanthanum atom in the Crystal Structure of the Class I Human Endoplasmic Reticulum 1,2- Alpha-Mannosidase and MAN9GLCNAC2-Pa Complex (pdb code 5kij). This binding sites where shown within 5.0 Angstroms radius around Lanthanum atom.
In total only one binding site of Lanthanum was determined in the Crystal Structure of the Class I Human Endoplasmic Reticulum 1,2- Alpha-Mannosidase and MAN9GLCNAC2-Pa Complex, PDB code: 5kij:

Lanthanum binding site 1 out of 1 in 5kij

Go back to Lanthanum Binding Sites List in 5kij
Lanthanum binding site 1 out of 1 in the Crystal Structure of the Class I Human Endoplasmic Reticulum 1,2- Alpha-Mannosidase and MAN9GLCNAC2-Pa Complex


Mono view


Stereo pair view

A full contact list of Lanthanum with other atoms in the La binding site number 1 of Crystal Structure of the Class I Human Endoplasmic Reticulum 1,2- Alpha-Mannosidase and MAN9GLCNAC2-Pa Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:La701

b:2.7
occ:1.00
 O A:HOH1038 2.4 4.1 1.0
O A:HOH864 2.5 3.0 1.0
O A:HOH1082 2.5 5.3 1.0
O A:HOH927 2.5 2.5 1.0
OG1 A:THR688 2.5 2.6 1.0
O3 A:MAN707 2.6 1.6 1.0
O A:THR688 2.6 1.9 1.0
O2 A:MAN707 2.6 2.0 1.0
O A:HOH892 2.7 2.2 1.0
C3 A:MAN707 3.5 4.1 1.0
C A:THR688 3.6 4.6 1.0
C2 A:MAN707 3.6 7.0 1.0
CB A:THR688 3.7 4.0 1.0
CA A:THR688 4.0 0.7 1.0
O A:HOH867 4.3 2.9 1.0
OE1 A:GLU663 4.3 1.4 1.0
C1 A:MAN707 4.3 8.0 1.0
O A:HOH834 4.3 2.8 1.0
OE1 A:GLU467 4.3 3.5 1.0
CG2 A:THR688 4.3 5.1 1.0
OE1 A:GLU602 4.4 3.0 1.0
O A:HOH989 4.4 2.3 1.0
OE2 A:GLU663 4.5 3.9 1.0
O A:HOH1048 4.7 0.9 1.0
OE2 A:GLU467 4.7 2.3 1.0
OE2 A:GLU602 4.8 5.4 1.0
OE2 A:GLU599 4.8 4.5 1.0
C6 A:MAN707 4.8 6.5 1.0
N A:GLU689 4.8 2.6 1.0
CD A:GLU663 4.8 3.6 1.0
C4 A:MAN707 4.9 7.1 1.0
CD A:GLU467 5.0 2.9 1.0
CD A:GLU602 5.0 2.2 1.0

Reference:

Y.Xiang, K.Karaveg, K.W.Moremen. Substrate Recognition and Catalysis By GH47 Alpha-Mannosidases Involved in Asn-Linked Glycan Maturation in the Mammalian Secretory Pathway. Proc. Natl. Acad. Sci. V. 113 E7890 2016U.S.A..
ISSN: ESSN 1091-6490
PubMed: 27856750
DOI: 10.1073/PNAS.1611213113
Page generated: Tue Aug 13 01:48:33 2024

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