8DMK: Laminin subunit alpha-1

Cryo-EM reveals the molecular basis of laminin polymerization and LN-lamininopathies. Determined by electron microscopy at 3.7 Å resolution. Released 1 Feb 2023.

Method
Electron microscopy
Resolution
3.7 Å
Organisms
Mus musculus, Homo sapiens
Chains
3
Atoms
7,348
Mol. weight
105.06 kDa
Ligands
CA, NAG
Released
1 Feb 2023

Explore 8DMK in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8DMK contains 30 α-helices and 65 β-strands across 3 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: 14 helices, 25 β-strands

ElementResiduesLengthSheet
β-strand2911
α-helix30-334
β-strand34-3522
β-strand41-4442
β-strand5013
β-strand5213
β-strand54-5744
α-helix62-643
β-strand73-7644
β-strand7715
β-strand8615
α-helix89-913
β-strand100-10126
α-helix102-1043
α-helix109-1124
β-strand114-132192
α-helix137-1393
β-strand141-14772
β-strand153-15972
α-helix163-1653
α-helix166-1705
α-helix1731
β-strand17412
α-helix175-1762
β-strand189-19022
β-strand203-20752
α-helix220-2256
β-strand227-237112
α-helix243-2464
α-helix258-2614
β-strand267-26826
β-strand27012
β-strand273-27752
β-strand28211
α-helix2871
β-strand288-28927
β-strand294-29527
β-strand30418
β-strand31018
Chain B: 7 helices, 20 β-strands
ElementResiduesLengthSheet
α-helix36-394
β-strand40-4129
β-strand50-52310
β-strand63111
β-strand78111
α-helix105-1095
β-strand112-11329
β-strand121-125510
β-strand131-132212
β-strand135-14069
β-strand147-152610
β-strand161-167710
α-helix170-1734
β-strand190-191210
β-strand204-20639
α-helix222-2254
β-strand229-230212
β-strand234-239610
α-helix255-2573
β-strand261-26999
β-strand271112
α-helix281-2833
β-strand305113
β-strand311113
β-strand325114
β-strand328114
α-helix331-3344
Chain G: 9 helices, 20 β-strands
ElementResiduesLengthSheet
β-strand50115
β-strand56116
β-strand63-65317
β-strand74-75218
α-helix80-823
β-strand91-92218
α-helix103-1053
β-strand118-119216
α-helix123-1253
β-strand128-1431617
β-strand147-152616
β-strand159-163517
β-strand174-179617
α-helix182-1854
β-strand204-206317
β-strand218-223616
α-helix234-2363
α-helix238-2447
β-strand246-2551017
α-helix261-2633
α-helix267-2704
β-strand276-283816
β-strand286117
β-strand291115
β-strand292-297619
β-strand303-307519
β-strand311-312220
β-strand318-319220
α-helix321-3233

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Laminin subunit alpha-1Aprotein305Mus musculusP19137
Laminin subunit beta-1Bprotein307Homo sapiensP07942 (AlphaFold model)
Laminin subunit gamma-1Gprotein305Homo sapiensP11047 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>8DMK_1 Laminin subunit alpha-1 (chains A)
GLFPAILNLATNAHISANATCGEKGPEMFCKLVEHVPGRPVRHAQCRVCDGNSTNPRERH
PISHAIDGTNNWWQSPSIQNGREYHWVTVTLDLRQVFQVAYIIIKAANAPRPGNWILERS
VDGVKFKPWQYYAVSDTECLTRYKITPRRGPPTYRADNEVICTSYYSKLVPLEHGEIHTS
LINGRPSADDPSPQLLEFTSARYIRLRLQRIRTLNADLMTLSHRDLRDLDPIVTRRYYYS
IKDISVGGMCICYGHASSCPWDEEAKQLQCQCEHNTCGESCDRCCPGYHQQPWRPGTISS
GNECE
Sequence of entity 2 (B), FASTA
>8DMK_2 Laminin subunit beta-1 (chains B)
GCAEGSCYPATGDLLIGRAQKLSVTSTCGLHKPEPYCIVSHLQEDKKCFICNSQDPYHET
LNPDSHLIENVVTTFAPNRLKIWWQSENGVENVTIQLDLEAEFHFTHLIMTFKTFRPAAM
LIERSSDFGKTWGVYRYFAYDCEASFPGISTGPMKKVDDIICDSRYSDIEPSTEGEVIFR
ALDPAFKIEDPYSPRIQNLLKITNLRIKFVKLHTLGDNLLDSRMEIREKYYYAVYDMVVR
GNCFCYGHASECAPVDGFNEEVEGMVHGHCMCRHNTKGLNCELCMDFYHDLPWRPAEGRN
SNACKKC
Sequence of entity 3 (G), FASTA
>8DMK_3 Laminin subunit gamma-1 (chains G)
MDECTDEGGRPQRCMPEFVNAAFNVTVVATNTCGTPPEEYCVQTGVTGVTKSCHLCDAGQ
PHLQHGAAFLTDYNNQADTTWWQSQTMLAGVQYPSSINLTLHLGKAFDITYVRLKFHTSR
PESFAIYKRTWEDGPWIPYQYYSGSCENTYSKANRGFIRTGGDEQQALCTDEFSDISPLT
GGNVAFSTLEGRPSAYNFDNSPVLQEWVTATDISVTLNRLNTFGDEVFNDPKVLKSYYYA
ISDFAVGGRCKCNGHASECMKNEFDKLVCNCKHNTYGVDCEKCLPFFNDRPWRRATAESA
SECLP

Ligands and cofactors

IDNameFormulaCopies
CACalcium ionCa1
NAG2-acetamido-2-deoxy-beta-D-glucopyranoseC8 H15 N O65

Primary citation

Cryo-EM reveals the molecular basis oflaminin polymerization and LN-lamininopathies. Kulczyk, A.W., McKee, K.K., Zhang, X. et al. Nat Commun (2023) 14:317-317. DOI 10.1038/s41467-023-36077-z · PubMed

Other PDB entries of the same protein (UniProt P19137), best resolution first:

Browse structure collections

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