5LFU: Myelin-associated glycoprotein

Myelin-associated glycoprotein (MAG) glycosylated and lysine-methylated full extracellular domain. Determined by X-ray diffraction at 4.3 Å resolution. Released 14 Dec 2016.

Method
X-ray diffraction
Resolution
4.3 Å
Organism
Mus musculus
Chains
1
Atoms
3,942
Mol. weight
57.74 kDa
Ligands
NAG, MAN
Released
14 Dec 2016

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

Secondary structure: helices and β-sheets

5LFU contains 6 α-helices and 47 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: 6 helices, 47 β-strands

ElementResiduesLengthSheet
β-strand23-2531
β-strand29-3242
β-strand38-4033
β-strand43-4531
β-strand55-6172
β-strand72-7542
β-strand7812
β-strand89-9133
α-helix95-973
β-strand9911
β-strand102-10433
α-helix109-1113
β-strand113-12192
β-strand126-12832
β-strand133-13752
β-strand142-14434
β-strand149-15025
β-strand155-16174
β-strand171-17556
α-helix1821
β-strand18314
α-helix1841
β-strand188-19144
β-strand195-204104
β-strand214-22076
β-strand227-23376
β-strand236-23725
β-strand241-24557
β-strand249-25248
β-strand257-26487
β-strand270-27458
β-strand282-28438
β-strand287-29267
β-strand301-30998
β-strand312-323128
α-helix325-3295
β-strand330-33349
β-strand343-34869
β-strand356-361610
β-strand364-369610
β-strand375-37959
α-helix384-3863
β-strand388-395810
β-strand401-407710
β-strand414-415211
β-strand420-423411
β-strand428-435811
β-strand441-445512
β-strand462-466511
β-strand469-476811
β-strand486-491612
β-strand496-501612
β-strand503111

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Myelin-associated glycoproteinAprotein500Mus musculusP20917 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>5LFU_1 Myelin-associated glycoprotein (chains A)
GSGHWGAWMPSTISAFEGTCVSIPCRFDFPDELRPAVVHGVWYFNSPYPKNYPPVVFKSR
TQVVHESFQGRSRLLGDLGLRNCTLLLSTLSPELGGKYYFRGDLGGYNQYTFSEHSVLDI
VNTPNIVVPPEVVAGTEVEVSCMVPDNCPELRPELSWLGHEGLGEPTVLGRLREDEGTWV
QVSLLHFVPTREANGHRLGCQAAFPNTTLQFEGYASLDVKYPPVIVEMNSSVEAIEGSHV
SLLCGADSNPPPLLTWMRDGMVLREAVAKSLYLDLEEVTPGEDGVYACLAENAYGQDNRT
VELSVMYAPWKPTVNGTVVAVEGETVSILCSTQSNPDPILTIFKEKQILATVIYESQLQL
ELPAVTPEDDGEYWCVAENQYGQRATAFNLSVEFAPIILLESHCAAARDTVQCLCVVKSN
PEPSVAFELPSRNVTVNETEREFVYSERSGLLLTSILTIRGQAQAPPRVICTSRNLYGTQ
SLELPFQGAHRAAAHHHHHH

Ligands and cofactors

IDNameFormulaCopies
NAG2-acetamido-2-deoxy-beta-D-glucopyranoseC8 H15 N O63
MANalpha-D-mannopyranoseC6 H12 O61

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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