1VFB: IgG1-kappa D1.3 fv

Bound water molecules and conformational stabilization help mediate an antigen-antibody association. Determined by X-ray diffraction at 1.8 Å resolution. Released 31 May 1994.

Method
X-ray diffraction
Resolution
1.8 Å
Organisms
Mus musculus, Gallus gallus
Chains
3
Atoms
2,779
Mol. weight
38.89 kDa
Released
31 May 1994

Explore 1VFB in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1VFB contains 12 α-helices and 32 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: 2 helices, 11 β-strands

ElementResiduesLengthSheet
β-strand4-741
β-strand10-1342
β-strand19-2571
β-strand33-3862
β-strand45-4952
β-strand53-5422
α-helix551
β-strand62-6761
β-strand70-7561
α-helix80-823
β-strand84-9072
β-strand9812
β-strand102-10652
Chain B: 2 helices, 12 β-strands
ElementResiduesLengthSheet
β-strand3-753
β-strand11-1224
β-strand18-2583
β-strand33-3975
β-strand46-5165
β-strand57-5935
α-helix64-663
β-strand67-7263
β-strand77-8263
α-helix87-893
β-strand91-9885
β-strand103-10645
β-strand110-11235
β-strand113-11424
Chain C: 8 helices, 9 β-strands
ElementResiduesLengthSheet
β-strand216
α-helix5-1410
β-strand2017
β-strand2317
α-helix25-3612
β-strand3916
β-strand43-4648
β-strand48-5368
β-strand58-5928
β-strand6519
β-strand7919
α-helix80-845
α-helix89-9810
α-helix104-1074
α-helix109-1102
α-helix111-1155
α-helix120-1234

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
IgG1-kappa D1.3 fv (light chain)Aprotein107Mus musculusP01635 (AlphaFold model)
IgG1-kappa D1.3 fv (heavy chain)Bprotein116Mus musculusP01820 (AlphaFold model)
Hen egg white lysozymeCprotein129Gallus gallusP00698 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1VFB_1 IGG1-KAPPA D1.3 FV (LIGHT CHAIN) (chains A)
DIVLTQSPASLSASVGETVTITCRASGNIHNYLAWYQQKQGKSPQLLVYYTTTLADGVPS
RFSGSGSGTQYSLKINSLQPEDFGSYYCQHFWSTPRTFGGGTKLEIK
Sequence of entity 2 (B), FASTA
>1VFB_2 IGG1-KAPPA D1.3 FV (HEAVY CHAIN) (chains B)
QVQLQESGPGLVAPSQSLSITCTVSGFSLTGYGVNWVRQPPGKGLEWLGMIWGDGNTDYN
SALKSRLSISKDNSKSQVFLKMNSLHTDDTARYYCARERDYRLDYWGQGTTLTVSS
Sequence of entity 3 (C), FASTA
>1VFB_3 HEN EGG WHITE LYSOZYME (chains C)
KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINS
RWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDV
QAWIRGCRL

Primary citation

Bound water molecules and conformational stabilization help mediate an antigen-antibody association. Bhat, T.N., Bentley, G.A., Boulot, G. et al. Proc Natl Acad Sci U S A (1994) 91:1089-1093. DOI 10.1073/pnas.91.3.1089 · PubMed

Other PDB entries of the same protein (UniProt P01635 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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