SMTL ID : 5lfu.1

Myelin-associated glycoprotein (MAG) glycosylated and lysine-methylated full extracellular domain

Coordinates

PDB Format

Method

X-RAY DIFFRACTION 4.30 Å

Oligo State

homo-dimer

Ligands

2 x NAG- NAG- BMA- MAN- MAN: alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose(Post Translational Modification)

NAG-NAG-BMA-MAN-MAN.1: 6 residues within 4Å: Chain A: L.75, G.76, N.82, T.84, P.149, E.150 No protein-ligand interaction detected (PLIP) NAG-NAG-BMA-MAN-MAN.8: 6 residues within 4Å: Chain B: L.75, G.76, N.82, T.84, P.149, E.150 No protein-ligand interaction detected (PLIP)

2 x NAG- FUC: alpha-L-fucopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose(Post Translational Modification)

NAG-FUC.2: 3 residues within 4Å: Chain A: T.313, V.314, N.315 2 PLIP interactions: 2 interactions with chain A Hydrophobic interactions: A:N.315 Hydrogen bonds: A:T.313 NAG-FUC.9: 3 residues within 4Å: Chain B: T.313, V.314, N.315 2 PLIP interactions: 2 interactions with chain B Hydrophobic interactions: B:N.315 Hydrogen bonds: B:T.313

2 x NAG- NAG: 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose(Non-functional Binders)(Post Translational Modification)

NAG-NAG.3: 3 residues within 4Å: Chain A: E.372, N.389 Ligands: NAG-NAG.10 No protein-ligand interaction detected (PLIP) NAG-NAG.10: 3 residues within 4Å: Chain B: E.372, N.389 Ligands: NAG-NAG.3 No protein-ligand interaction detected (PLIP)

2 x MAN: alpha-D-mannopyranose(Non-covalent)(Non-functional Binders)

MAN.4: 3 residues within 4Å: Chain A: H.4, W.5, P.30 2 PLIP interactions: 2 interactions with chain A Hydrogen bonds: A:W.5, A:W.5 MAN.11: 3 residues within 4Å: Chain B: H.4, W.5, P.30 2 PLIP interactions: 2 interactions with chain B Hydrogen bonds: B:W.5, B:W.5

6 x NAG: 2-acetamido-2-deoxy-beta-D-glucopyranose(Non-covalent)(Non-functional Binders)(Post Translational Modification)

NAG.5: 2 residues within 4Å: Chain A: P.205, N.206 No protein-ligand interaction detected (PLIP) NAG.6: 4 residues within 4Å: Chain A: N.229, S.230, V.232, S.241 1 PLIP interactions: 1 interactions with chain A Hydrogen bonds: A:S.230 NAG.7: 2 residues within 4Å: Chain A: L.289, N.298 1 PLIP interactions: 1 interactions with chain A Hydrogen bonds: A:N.298 NAG.12: 2 residues within 4Å: Chain B: P.205, N.206 No protein-ligand interaction detected (PLIP) NAG.13: 4 residues within 4Å: Chain B: N.229, S.230, V.232, S.241 1 PLIP interactions: 1 interactions with chain B Hydrogen bonds: B:S.230 NAG.14: 2 residues within 4Å: Chain B: L.289, N.298 1 PLIP interactions: 1 interactions with chain B Hydrogen bonds: B:N.298

Links

RCSB   PDBe   PDBj   PDBsum   CATH   PLIP

Citation

Pronker, M.F. et al., Structural basis of myelin-associated glycoprotein adhesion and signalling. Nat Commun (2016)

Release Date

2016-12-14

Peptides

Myelin-associated glycoprotein: AB

SMTL:PDB

SMTL Chain Id:
PDB Chain Id:

A
A

B
A

Myelin-associated glycoprotein

Related Entries With Identical Sequence