5LFV: Myelin-associated glycoprotein

Crystal structure of glycosylated Myelin-associated glycoprotein (MAG) Ig1-3 with soaked trisaccharide ligand. Determined by X-ray diffraction at 2.3 Å resolution. Released 14 Dec 2016.

Method
X-ray diffraction
Resolution
2.3 Å
Organism
Mus musculus
Chains
2
Atoms
5,095
Mol. weight
74.62 kDa
Ligands
NAG, MAN
Released
14 Dec 2016

Explore 5LFV in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5LFV contains 17 α-helices and 58 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 12 helices, 28 β-strands

ElementResiduesLengthSheet
β-strand23-2531
β-strand29-3352
β-strand38-4033
β-strand43-4531
α-helix48-503
β-strand56-6162
α-helix70-712
β-strand72-7542
β-strand89-9133
α-helix95-973
β-strand9911
β-strand102-10433
α-helix109-1113
β-strand113-12082
β-strand126-138132
α-helix1411
β-strand142-14434
β-strand149-15025
β-strand155-16284
α-helix169-1702
β-strand171-17556
α-helix178-1803
β-strand184-19074
α-helix192-1943
β-strand196-20494
α-helix208-2103
β-strand214-22076
β-strand227-23376
β-strand236-23725
β-strand238-24587
β-strand249-25248
β-strand257-266107
α-helix268-2692
β-strand270-27568
β-strand278-28478
β-strand287-29267
α-helix297-2993
β-strand301-30998
β-strand312-324138
α-helix325-3284
Chain B: 5 helices, 30 β-strands
ElementResiduesLengthSheet
β-strand23-2539
β-strand29-33510
β-strand38-40311
β-strand43-4539
β-strand56-61610
α-helix66-683
β-strand72-75410
α-helix83-853
β-strand89-92411
β-strand9919
β-strand101-104411
α-helix109-1113
β-strand113-120810
β-strand126-128310
β-strand133-138610
β-strand142-144312
β-strand149-150213
β-strand155-162812
β-strand171-175514
β-strand184-189612
β-strand197-204812
α-helix208-2103
β-strand214-220714
β-strand227-233714
β-strand236-237213
β-strand238-245815
β-strand249-252416
β-strand257-2661015
β-strand270-275617
β-strand278-284717
β-strand287-292615
β-strand302-309817
β-strand312-319817
β-strand320-324516
α-helix325-3284

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Myelin-associated glycoproteinA, Bprotein317Mus musculusP20917 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>5LFV_1 Myelin-associated glycoprotein (chains A, B)
GSGHWGAWMPSTISAFEGTCVSIPCRFDFPDELRPAVVHGVWYFNSPYPKNYPPVVFKSR
TQVVHESFQGRSRLLGDLGLRNCTLLLSTLSPELGGKYYFRGDLGGYNQYTFSEHSVLDI
VNTPNIVVPPEVVAGTEVEVSCMVPDNCPELRPELSWLGHEGLGEPTVLGRLREDEGTWV
QVSLLHFVPTREANGHRLGCQAAFPNTTLQFEGYASLDVKYPPVIVEMNSSVEAIEGSHV
SLLCGADSNPPPLLTWMRDGMVLREAVAKSLYLDLEEVTPGEDGVYACLAENAYGQDNRT
VELSVMYAAAAHHHHHH

Ligands and cofactors

IDNameFormulaCopies
NAG2-acetamido-2-deoxy-beta-D-glucopyranoseC8 H15 N O65
MANalpha-D-mannopyranoseC6 H12 O62

Water and common crystallization additives (SO4, GOL) are not listed.

Primary citation

Structural basis of myelin-associated glycoprotein adhesion and signalling. Pronker, M.F., Lemstra, S., Snijder, J. et al. Nat Commun (2016) 7:13584-13584. DOI 10.1038/ncomms13584 · PubMed

Other PDB entries of the same protein (UniProt P20917 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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