Manganese in PDB 8v9q: Crystal Structure of Mgalnac-T1 in Complex with the Mucin Glycopeptide MUC5AC-13, MN2+, and Udp.

The structure of Crystal Structure of Mgalnac-T1 in Complex with the Mucin Glycopeptide MUC5AC-13, MN2+, and Udp., PDB code: 8v9q was solved by N.L.Samara, A.M.Collette, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.90 / 2.29
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	59.635, 72.761, 148.498, 90, 95.44, 90
R / Rfree (%)	24.8 / 27.8

The binding sites of Manganese atom in the Crystal Structure of Mgalnac-T1 in Complex with the Mucin Glycopeptide MUC5AC-13, MN2+, and Udp. (pdb code 8v9q). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Crystal Structure of Mgalnac-T1 in Complex with the Mucin Glycopeptide MUC5AC-13, MN2+, and Udp., PDB code: 8v9q:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Crystal Structure of Mgalnac-T1 in Complex with the Mucin Glycopeptide MUC5AC-13, MN2+, and Udp.


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 Mgalnac-T1 in Complex with the Mucin Glycopeptide MUC5AC-13, MN2+, and Udp. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn607 b:25.7 occ:1.00 O1B A:UDP601 2.1 23.8 1.0 NE2 A:HIS211 2.1 21.7 1.0 OD2 A:ASP209 2.2 31.8 1.0 O1A A:UDP601 2.2 51.4 1.0 NE2 A:HIS344 2.2 27.6 1.0 O A:HOH746 2.2 31.2 1.0 CE1 A:HIS211 2.9 30.0 1.0 HE1 A:HIS211 3.0 36.0 1.0 CE1 A:HIS344 3.1 20.5 1.0 H5'1 A:UDP601 3.2 56.2 1.0 HE1 A:HIS344 3.2 24.6 1.0 PB A:UDP601 3.2 35.5 1.0 CD2 A:HIS211 3.3 23.5 1.0 CD2 A:HIS344 3.3 27.2 1.0 CG A:ASP209 3.3 32.7 1.0 PA A:UDP601 3.5 63.5 1.0 HD2 A:HIS344 3.5 32.6 1.0 HD2 A:HIS211 3.5 28.2 1.0 O2B A:UDP601 3.6 22.9 1.0 HB3 A:ASP209 3.6 36.9 1.0 H3' A:UDP601 3.7 50.5 1.0 O3A A:UDP601 3.7 30.8 1.0 CB A:ASP209 3.9 30.8 1.0 HH22 A:ARG347 4.0 42.3 1.0 HB2 A:ASP209 4.0 36.9 1.0 O A:HOH780 4.1 50.8 1.0 ND1 A:HIS211 4.1 24.5 1.0 C5' A:UDP601 4.1 46.8 1.0 ND1 A:HIS344 4.3 28.7 1.0 CG A:HIS211 4.3 21.9 1.0 O5' A:UDP601 4.3 51.1 1.0 OD1 A:ASP209 4.4 33.1 1.0 CG A:HIS344 4.4 24.6 1.0 O A:VAL345 4.5 21.7 1.0 O3B A:UDP601 4.5 18.8 1.0 O2A A:UDP601 4.6 40.4 1.0 C3' A:UDP601 4.6 42.1 1.0 NH2 A:ARG347 4.7 35.3 1.0 HE A:ARG347 4.7 44.9 1.0 C4' A:UDP601 4.8 38.8 1.0 HD1 A:HIS211 4.9 29.4 1.0 O A:HOH736 4.9 32.6 1.0 H5'2 A:UDP601 4.9 56.2 1.0 H4' A:UDP601 4.9 46.6 1.0

Manganese binding site 2 out of 2 in the Crystal Structure of Mgalnac-T1 in Complex with the Mucin Glycopeptide MUC5AC-13, MN2+, and Udp.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of Mgalnac-T1 in Complex with the Mucin Glycopeptide MUC5AC-13, MN2+, and Udp. within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn604 b:143.0 occ:1.00 HH11 B:ARG347 2.0 183.9 1.0 O1B B:UDP601 2.0 140.2 1.0 NE2 B:HIS211 2.2 189.5 1.0 NE2 B:HIS344 2.3 138.2 1.0 O2B B:UDP601 2.5 137.2 1.0 O1A B:UDP601 2.5 125.5 1.0 NH1 B:ARG347 2.6 153.3 1.0 HH12 B:ARG347 2.6 183.9 1.0 HD2 B:HIS211 2.7 209.2 1.0 PB B:UDP601 2.7 147.5 1.0 CD2 B:HIS211 2.8 174.3 1.0 HE1 B:HIS344 2.9 151.2 1.0 CE1 B:HIS344 2.9 126.0 1.0 CE1 B:HIS211 3.4 188.3 1.0 CD2 B:HIS344 3.5 127.1 1.0 O3A B:UDP601 3.5 138.3 1.0 PA B:UDP601 3.6 152.1 1.0 CZ B:ARG347 3.7 124.6 1.0 HE1 B:HIS211 3.8 225.9 1.0 OD2 B:ASP209 3.8 151.5 1.0 O B:VAL345 3.8 151.3 1.0 HD2 B:HIS344 3.8 152.5 1.0 HH21 B:ARG347 3.9 148.3 1.0 CG B:HIS211 4.0 171.6 1.0 O3B B:UDP601 4.0 121.6 1.0 ND1 B:HIS344 4.1 125.7 1.0 HG3 B:ARG347 4.2 167.4 1.0 H5'1 B:UDP601 4.2 151.2 1.0 NH2 B:ARG347 4.2 123.6 1.0 ND1 B:HIS211 4.3 166.0 1.0 O2A B:UDP601 4.3 123.2 1.0 CG B:HIS344 4.4 128.8 1.0 HA B:PHE346 4.5 161.6 1.0 HB3 B:ASP209 4.5 187.9 1.0 C B:VAL345 4.7 152.5 1.0 HD2 B:ARG347 4.7 153.5 1.0 NE B:ARG347 4.8 126.9 1.0 HG22 F:THR2 4.8 149.6 1.0 CG B:ASP209 4.8 153.2 1.0 HG21 F:THR2 4.8 149.6 1.0 HD1 B:HIS344 4.8 150.8 1.0 O5' B:UDP601 4.9 129.1 1.0 H3' B:UDP601 5.0 152.6 1.0

A.M.Collette, S.A.Hassan, S.I.Schmidt, A.J.Lara, W.Yang, N.L.Samara. An Unusual Dual Sugar-Binding Lectin Domain Controls the Substrate Specificity of A Mucin-Type O-Glycosyltransferase. Sci Adv V. 10 J8829 2024.
ISSN: ESSN 2375-2548
PubMed: 38416819
DOI: 10.1126/SCIADV.ADJ8829