SMTL ID : 3qdx.1 (2 other biounits)

Structure of the orthorhombic form of the Boletus edulis lectin in complex with T-antigen disaccharide and N,N-diacetyl chitobiose

Coordinates

PDB Format

Method

X-RAY DIFFRACTION 1.70 Å

Oligo State

homo-tetramer

Ligands

4 x A2G- GAL: beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-alpha-D-galactopyranose(Non-covalent)

A2G-GAL.1: 9 residues within 4Å: Chain A: Y.29, A.30, S.49, G.50, H.72, N.73, Y.74, Y.98, R.107 4 PLIP interactions: 4 interactions with chain A Hydrophobic interactions: A:Y.74 Hydrogen bonds: A:G.50, A:N.73, A:R.107, A:R.107, A:A.30, A:S.49 Salt bridges: A:H.72 Water bridges: A:H.28, A:N.31 A2G-GAL.2: 9 residues within 4Å: Chain B: Y.29, A.30, S.49, G.50, H.72, N.73, Y.74, Y.98, R.107 4 PLIP interactions: 4 interactions with chain B Hydrogen bonds: B:G.50, B:N.73, B:R.107, B:R.107, B:A.30, B:S.49 Water bridges: B:N.73, B:N.73, B:H.28, B:N.31 Salt bridges: B:H.72 A2G-GAL.5: 9 residues within 4Å: Chain C: Y.29, A.30, S.49, G.50, H.72, N.73, Y.74, Y.98, R.107 4 PLIP interactions: 4 interactions with chain C Hydrophobic interactions: C:Y.74 Hydrogen bonds: C:G.50, C:N.73, C:R.107, C:R.107, C:A.30, C:S.49 Salt bridges: C:H.72 Water bridges: C:H.28, C:N.31 A2G-GAL.6: 9 residues within 4Å: Chain D: Y.29, A.30, S.49, G.50, H.72, N.73, Y.74, Y.98, R.107 4 PLIP interactions: 4 interactions with chain D Hydrogen bonds: D:G.50, D:N.73, D:R.107, D:R.107, D:A.30, D:S.49 Water bridges: D:N.73, D:N.73, D:H.28, D:N.31 Salt bridges: D:H.72

4 x NAG- NAG: 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose(Non-covalent)

NAG-NAG.3: 9 residues within 4Å: Chain A: D.79, V.80, V.81, T.82, R.103, Y.105, T.106, Y.114, V.116 7 PLIP interactions: 7 interactions with chain A Hydrophobic interactions: A:V.116 Hydrogen bonds: A:T.82, A:Y.97, A:Y.97, A:R.103, A:Y.105, A:Y.114 NAG-NAG.4: 9 residues within 4Å: Chain B: D.79, V.80, V.81, T.82, R.103, Y.105, T.106, Y.114, V.116 4 PLIP interactions: 4 interactions with chain B Hydrophobic interactions: B:V.116 Hydrogen bonds: B:T.82, B:R.103, B:Y.114 NAG-NAG.7: 9 residues within 4Å: Chain C: D.79, V.80, V.81, T.82, R.103, Y.105, T.106, Y.114, V.116 7 PLIP interactions: 7 interactions with chain C Hydrophobic interactions: C:V.116 Hydrogen bonds: C:T.82, C:Y.97, C:R.103, C:T.106, C:Y.114, C:Y.114 NAG-NAG.8: 9 residues within 4Å: Chain D: D.79, V.80, V.81, T.82, R.103, Y.105, T.106, Y.114, V.116 6 PLIP interactions: 6 interactions with chain D Hydrophobic interactions: D:V.116 Hydrogen bonds: D:T.82, D:R.103, D:T.106, D:Y.114, D:Y.114

Links

RCSB   PDBe   PDBj   PDBsum   CATH   PLIP

Citation

Bovi, M. et al., Structure of a lectin with antitumoral properties in king bolete (Boletus edulis) mushrooms. Glycobiology (2011)

Release Date

2011-02-23

Peptides

BOLETUS EDULIS LECTIN: ABCD

SMTL:PDB

SMTL Chain Id:
PDB Chain Id:

A
A

B
B

C
A

D
B

BOLETUS EDULIS LECTIN

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