Zinc in PDB 1x1v: Structure of Banana Lectin- Methyl-Alpha-Mannose Complex

The structure of Structure of Banana Lectin- Methyl-Alpha-Mannose Complex, PDB code: 1x1v was solved by D.D.Singh, K.Saikrishnan, P.Kumar, A.Surolia, K.Sekar, M.Vijayan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	24.92 / 2.45
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	80.820, 80.820, 148.000, 90.00, 90.00, 120.00
R / Rfree (%)	22.4 / 26

The binding sites of Zinc atom in the Structure of Banana Lectin- Methyl-Alpha-Mannose Complex (pdb code 1x1v). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the Structure of Banana Lectin- Methyl-Alpha-Mannose Complex, PDB code: 1x1v:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in the Structure of Banana Lectin- Methyl-Alpha-Mannose Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Banana Lectin- Methyl-Alpha-Mannose Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn901 b:58.3 occ:1.00 OD1 A:ASP41 2.2 47.9 1.0 ND1 A:HIS54 2.3 55.3 1.0 OD2 A:ASP41 2.3 47.3 1.0 O A:HOH449 2.5 55.0 1.0 O A:HOH448 2.6 65.3 1.0 CG A:ASP41 2.6 46.3 1.0 CG A:HIS54 2.7 54.4 1.0 CB A:HIS54 2.9 53.7 1.0 CE1 A:HIS54 3.3 55.5 1.0 CD2 A:HIS54 3.8 55.6 1.0 NE2 A:HIS54 4.0 55.2 1.0 CB A:ASP41 4.1 45.7 1.0 CE2 A:PHE32 4.2 40.3 1.0 CA A:HIS54 4.3 53.5 1.0 CZ A:PHE32 4.7 40.1 1.0 CA A:ASP41 4.9 45.5 1.0

Zinc binding site 2 out of 3 in the Structure of Banana Lectin- Methyl-Alpha-Mannose Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of Banana Lectin- Methyl-Alpha-Mannose Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn903 b:83.2 occ:1.00 CD2 A:HIS63 2.4 47.8 1.0 CG A:HIS63 3.0 47.1 1.0 CB A:HIS63 3.2 46.2 1.0 NE2 A:HIS63 3.5 48.1 1.0 CA A:HIS63 3.5 45.9 1.0 O A:PRO62 3.7 45.3 1.0 O4 A:MMA805 3.7 62.8 1.0 ND1 A:HIS63 4.1 48.4 1.0 CE1 A:HIS63 4.3 48.5 1.0 N A:HIS63 4.4 45.7 1.0 C A:PRO62 4.4 45.5 1.0 CE2 A:PHE104 4.6 46.4 1.0 C6 A:MMA805 4.6 63.1 1.0 C A:HIS63 4.7 45.7 1.0 C4 A:MMA805 4.9 62.7 1.0 N A:GLU64 5.0 45.9 1.0 C5 A:MMA805 5.0 62.9 1.0

Zinc binding site 3 out of 3 in the Structure of Banana Lectin- Methyl-Alpha-Mannose Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Structure of Banana Lectin- Methyl-Alpha-Mannose Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn902 b:52.5 occ:1.00 OD2 B:ASP41 2.0 46.6 1.0 ND1 B:HIS54 2.1 58.0 1.0 OD1 B:ASP41 2.3 47.4 1.0 CG B:ASP41 2.5 48.0 1.0 O B:HOH450 2.9 52.1 1.0 CE1 B:HIS54 3.0 58.2 1.0 CG B:HIS54 3.1 57.9 1.0 CB B:HIS54 3.5 57.7 1.0 CA B:HIS54 3.9 58.0 1.0 CB B:ASP41 4.0 48.5 1.0 CE2 B:PHE32 4.2 50.9 1.0 NE2 B:HIS54 4.2 58.8 1.0 CD2 B:HIS54 4.2 58.2 1.0 CZ B:PHE32 4.4 50.8 1.0 O B:HOH275 4.6 59.6 1.0 N B:HIS54 4.9 58.6 1.0 CA B:ASP41 4.9 48.7 1.0 CD2 B:PHE32 4.9 50.7 1.0 C B:HIS54 4.9 57.2 1.0

D.D.Singh, K.Saikrishnan, P.Kumar, A.Surolia, K.Sekar, M.Vijayan. Unusual Sugar Specificity of Banana Lectin From Musa Paradisiaca and Its Probable Evolutionary Origin. Crystallographic and Modelling Studies Glycobiology V. 15 1025 2005.
ISSN: ISSN 0959-6658
PubMed: 15958419
DOI: 10.1093/GLYCOB/CWI087