9AZ3: Laminin subunit gamma-1

Cryo-EM reveals molecular mechanisms underlying the inhibitory effect of netrin-4 on laminin matrix formation. Determined by electron microscopy at 3.9 Å resolution. Released 20 Aug 2025.

Method
Electron microscopy
Resolution
3.9 Å
Organisms
Homo sapiens, Mus musculus
Chains
2
Atoms
4,203
Mol. weight
67.88 kDa
Ligands
NAG
Released
20 Aug 2025

Explore 9AZ3 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9AZ3 contains 13 α-helices and 37 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 G: 6 helices, 18 β-strands

ElementResiduesLengthSheet
β-strand55-5621
β-strand63-6422
β-strand76-7723
β-strand89-9023
α-helix103-1064
β-strand118-11921
α-helix123-1253
β-strand134-13742
β-strand14314
β-strand14415
β-strand147-15261
β-strand159-16572
β-strand172-17982
α-helix182-1854
β-strand20612
β-strand21811
β-strand221-22331
α-helix234-2363
α-helix238-2447
β-strand24515
β-strand248-25252
α-helix267-2726
β-strand276-28491
β-strand28614
Chain N: 7 helices, 19 β-strands
ElementResiduesLengthSheet
β-strand4916
β-strand6117
β-strand6618
β-strand7218
β-strand7817
β-strand8119
β-strand8819
α-helix91-933
α-helix103-1053
β-strand11716
β-strand125-126210
β-strand130111
α-helix137-1393
β-strand142-146512
β-strand158112
α-helix164-1674
β-strand198111
α-helix203-2053
α-helix213-2164
α-helix217-2193
β-strand220-221210
β-strand224-228512
β-strand271113
β-strand293113
β-strand299-300214
β-strand306-307214

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Laminin subunit gamma-1Gprotein305Homo sapiensP11047 (AlphaFold model)
Netrin-4Nprotein284Mus musculusQ9JI33 (AlphaFold model)
Sequence of entity 1 (G), FASTA
>9AZ3_1 Laminin subunit gamma-1 (chains G)
MDECTDEGGRPQRCMPEFVNAAFNVTVVATNTCGTPPEEYCVQTGVTGVTKSCHLCDAGQ
PHLQHGAAFLTDYNNQADTTWWQSQTMLAGVQYPSSINLTLHLGKAFDITYVRLKFHTSR
PESFAIYKRTWEDGPWIPYQYYSGSCENTYSKANRGFIRTGGDEQQALCTDEFSDISPLT
GGNVAFSTLEGRPSAYNFDNSPVLQEWVTATDISVTLNRLNTFGDEVFNRPKVLKSYYYA
ISDFAVGGRCKCNGHASECMKNEFDKLVCNCKHNTYGVDCEKCLPFFNDRPWRRATAESA
SECLP
Sequence of entity 2 (N), FASTA
>9AZ3_2 Netrin-4 (chains N)
LGRKLRADTMCGQNATELFCFYSENADLTCRQPKCDKCNAAHSHLAHPPSAMADSSFRFP
RTWWQSAEDVHREKIQLDLEAEFYFTHLIMVFKSPRPAAMVLDRSQDFGKTWKPYKYFAT
NCSATFGLEDDVVKKGAICTSRYSNPFPCTGGEVIFRALSPPYDIENPYSAKVQEQLKIT
NLRVRLLKRQSCPCQINDLNAKPHHFMHYAVYDFIVKGSCFCNGHADQCLPVEGFRPIKA
PGAFHVVHGRCMCKHNTAGSHCQHCAPLYNDRPWEAADGRTGAP

Ligands and cofactors

IDNameFormulaCopies
NAG2-acetamido-2-deoxy-beta-D-glucopyranoseC8 H15 N O67

Primary citation

Cryo-EM reveals molecular mechanisms underlying the inhibitory effect of netrin-4 on laminin matrix formation. Kulczyk, A.W., McKee, K.K., Yurchenco, P.D. Nat Commun (2025) 16:7256-7256. DOI 10.1038/s41467-025-62814-7 · PubMed

Other PDB entries of the same protein (UniProt P11047 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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