- Coordinates
- PDB Format
- Method
- X-RAY DIFFRACTION 1.99 Å
- Oligo State
- homo-dimer
- Ligands
- 4 x NAG- GAL- FUC: alpha-L-fucopyranose-(1-2)-beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose(Non-functional Binders)(Non-covalent)
- 3 x NDG- GAL- FUC- FUC: alpha-L-fucopyranose-(1-2)-beta-D-galactopyranose-(1-4)-[alpha-L-fucopyranose-(1-3)]2-acetamido-2-deoxy-alpha-D-glucopyranose(Non-functional Binders)
NDG-GAL-FUC-FUC.3: 12 residues within 4Å:- Chain A: L.117, Q.124, R.126, E.138, M.140, N.142, T.150, P.174, I.176, Y.192, G.197, W.198
1 PLIP interactions:1 interactions with chain A- Hydrophobic interactions: A:L.117, A:I.176, A:Y.192
- Hydrogen bonds: A:R.126, A:E.138, A:T.150, A:T.150, A:T.150, A:R.126, A:R.126, A:N.142
- Water bridges: A:Q.124, A:W.198
NDG-GAL-FUC-FUC.4: 9 residues within 4Å:- Chain A: N.22, L.24, Y.40, W.44, D.280, R.282, E.296, N.300, H.303
4 PLIP interactions:4 interactions with chain A- Hydrogen bonds: A:N.300, A:Y.40, A:N.22, A:N.300
- Water bridges: A:Y.40, A:N.300
- Salt bridges: A:R.282
NDG-GAL-FUC-FUC.7: 12 residues within 4Å:- Chain B: L.117, Q.124, R.126, E.138, M.140, N.142, T.150, P.174, I.176, Y.192, G.197, W.198
1 PLIP interactions:1 interactions with chain B- Hydrophobic interactions: B:I.176, B:Y.192
- Hydrogen bonds: B:R.126, B:E.138, B:T.150, B:T.150, B:T.150, B:R.126, B:N.142, B:Y.192
- 1 x GAL- FUC: alpha-L-fucopyranose-(1-2)-beta-D-galactopyranose
- 2 x GOL: GLYCEROL
GOL.9: 5 residues within 4Å:- Chain B: Y.168, R.177, Q.189, M.229, W.245
6 PLIP interactions:6 interactions with chain B- Hydrogen bonds: B:Y.168, B:Y.168, B:R.177, B:Q.189, B:Q.189
- Water bridges: B:Y.199
GOL.10: 5 residues within 4Å:- Chain A: Y.168, R.177, Q.189, M.229, W.245
4 PLIP interactions:4 interactions with chain A- Hydrogen bonds: A:Y.168, A:Y.168, A:R.177, A:Q.189
- 2 x FUC: alpha-L-fucopyranose(Non-covalent)
FUC.11: 6 residues within 4Å:- Chain A: R.230, Q.242, F.274, P.279, L.281, W.299
8 PLIP interactions:8 interactions with chain A- Hydrophobic interactions: A:F.274, A:P.279, A:L.281, A:W.299
- Hydrogen bonds: A:R.230, A:Q.242, A:Q.242
- Salt bridges: A:R.230
FUC.12: 7 residues within 4Å:- Chain B: R.230, Q.242, C.244, F.274, P.279, L.281, W.299
8 PLIP interactions:8 interactions with chain B- Hydrophobic interactions: B:F.274, B:P.279, B:L.281, B:W.299
- Hydrogen bonds: B:R.230, B:Q.242, B:Q.242
- Salt bridges: B:R.230
- Links
- RCSB PDBe PDBj PDBsum CATH PLIP
- Citation
- Houser, J. et al., Structural Insights Into Aspergillus Fumigatus Lectin Specificity: Afl Binding Sites are Functionally Non-Equivalent. Acta Crystallogr.,Sect.D (2015)
- Release Date
- 2015-03-11
- Peptides
- FUCOSE-SPECIFIC LECTIN FLEA: AB
- SMTL:PDB
- SMTL Chain Id:
PDB Chain Id:A
AB
B
- Coordinates
- PDB Format
- Method
- X-RAY DIFFRACTION 1.99 Å
- Oligo State
- homo-dimer
- Ligands
- 4 x NAG- GAL- FUC: alpha-L-fucopyranose-(1-2)-beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose(Non-functional Binders)(Non-covalent)
- 3 x NDG- GAL- FUC- FUC: alpha-L-fucopyranose-(1-2)-beta-D-galactopyranose-(1-4)-[alpha-L-fucopyranose-(1-3)]2-acetamido-2-deoxy-alpha-D-glucopyranose(Non-functional Binders)
- 1 x GAL- FUC: alpha-L-fucopyranose-(1-2)-beta-D-galactopyranose
- 2 x GOL: GLYCEROL
- 2 x FUC: alpha-L-fucopyranose(Non-covalent)
- Links
- RCSB PDBe PDBj PDBsum CATH PLIP
- Citation
- Houser, J. et al., Structural Insights Into Aspergillus Fumigatus Lectin Specificity: Afl Binding Sites are Functionally Non-Equivalent. Acta Crystallogr.,Sect.D (2015)
- Release Date
- 2015-03-11
- Peptides
- FUCOSE-SPECIFIC LECTIN FLEA: AB
- SMTL:PDB
- SMTL Chain Id:
PDB Chain Id:A
AB
B