5LF5: Myelin-associated glycoprotein

Myelin-associated glycoprotein (MAG) deglycosylated full extracellular domain with co-purified ligand. Determined by X-ray diffraction at 3.8 Å resolution. Released 14 Dec 2016.

Method
X-ray diffraction
Resolution
3.8 Å
Organism
Mus musculus
Chains
1
Atoms
3,887
Mol. weight
57.3 kDa
Ligands
MAN, NAG
Released
14 Dec 2016

Explore 5LF5 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5LF5 contains 9 α-helices and 48 β-strands across 1 chain. 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: 9 helices, 48 β-strands

ElementResiduesLengthSheet
β-strand23-2531
β-strand29-3352
β-strand38-4033
β-strand43-4531
β-strand56-6162
α-helix69-713
β-strand72-7542
β-strand89-9133
α-helix95-973
β-strand102-10433
α-helix109-1113
β-strand113-12082
β-strand126-12832
β-strand133-13862
β-strand142-14434
β-strand149-15025
β-strand155-16284
β-strand171-17556
α-helix181-1822
β-strand183-19194
β-strand195-204104
α-helix208-2103
β-strand214-22076
β-strand227-23376
β-strand236-23725
β-strand241-24557
β-strand249-25248
β-strand256-26497
α-helix268-2692
β-strand270-27458
β-strand27519
β-strand27819
β-strand282-28328
β-strand287-29377
β-strand301-30998
β-strand312-323128
α-helix325-3295
β-strand330-333410
β-strand336-338311
β-strand343-348610
β-strand357-361512
β-strand364-369612
β-strand374-379610
α-helix384-3863
β-strand388-394712
β-strand401-407712
β-strand408-410311
β-strand414-415213
β-strand420-423413
β-strand428-435813
β-strand441-445514
β-strand460-466713
β-strand469-476813
α-helix483-4853
β-strand487-491514
β-strand496-500514
β-strand503113

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Myelin-associated glycoproteinAprotein500Mus musculusP20917 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>5LF5_1 Myelin-associated glycoprotein (chains A)
GSGHWGAWMPSTISAFEGTCVSIPCRFDFPDELRPAVVHGVWYFNSPYPKNYPPVVFKSR
TQVVHESFQGRSRLLGDLGLRNCTLLLSTLSPELGGKYYFRGDLGGYNQYTFSEHSVLDI
VNTPNIVVPPEVVAGTEVEVSCMVPDNCPELRPELSWLGHEGLGEPTVLGRLREDEGTWV
QVSLLHFVPTREANGHRLGCQAAFPNTTLQFEGYASLDVKYPPVIVEMNSSVEAIEGSHV
SLLCGADSNPPPLLTWMRDGMVLREAVAKSLYLDLEEVTPGEDGVYACLAENAYGQDNRT
VELSVMYAPWKPTVNGTVVAVEGETVSILCSTQSNPDPILTIFKEKQILATVIYESQLQL
ELPAVTPEDDGEYWCVAENQYGQRATAFNLSVEFAPIILLESHCAAARDTVQCLCVVKSN
PEPSVAFELPSRNVTVNETEREFVYSERSGLLLTSILTIRGQAQAPPRVICTSRNLYGTQ
SLELPFQGAHRAAAHHHHHH

Ligands and cofactors

IDNameFormulaCopies
MANalpha-D-mannopyranoseC6 H12 O61
NAG2-acetamido-2-deoxy-beta-D-glucopyranoseC8 H15 N O64

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:

Browse structure collections

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