4PZ5: Second and third fibronectin F1 modules

Crystal structure of the second and third fibronectin F1 modules in complex with a fragment of BBK32 from Borrelia burgdorferi. Determined by X-ray diffraction at 1.96 Å resolution. Released 2 Jul 2014.

Method
X-ray diffraction
Resolution
1.96 Å
Organisms
Homo sapiens, Borrelia burgdorferi
Chains
2
Atoms
958
Mol. weight
11.98 kDa
Released
2 Jul 2014

Explore 4PZ5 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4PZ5 contains 0 α-helices and 11 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: 0 helices, 10 β-strands

ElementResiduesLengthSheet
β-strand65-6841
β-strand73-7641
β-strand80-8562
β-strand88-9692
β-strand101-10552
β-strand109-11023
β-strand117-11823
β-strand122-12654
β-strand133-14084
β-strand145-15064
Chain B: 0 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand180-18342

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
FibronectinAprotein90Homo sapiensP02751 (AlphaFold model)
Fibronectin-binding protein BBK32Bprotein16Borrelia burgdorferiO50835 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>4PZ5_1 Fibronectin (chains A)
AEETCFDKYTGNTYRVGDTYERPKDSMIWDCTCIGAGRGRISCTIANRCHEGGQSYKIGD
TWRRPHETGGYMLECVCLGNGKGEWTCKPI
Sequence of entity 2 (B), FASTA
>4PZ5_2 Fibronectin-binding protein BBK32 (chains B)
XSISYTDEIEEEDYDQ

Primary citation

Borrelia burgdorferi Protein BBK32 Binds to Soluble Fibronectin via the N-terminal 70-kDa Region, Causing Fibronectin to Undergo Conformational Extension. Harris, G., Ma, W., Maurer, L.M. et al. J Biol Chem (2014) 289:22490-22499. DOI 10.1074/jbc.M114.578419 · PubMed

Other PDB entries of the same protein (UniProt P02751 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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