1WZ1: Fv fragment

Crystal structure of the Fv fragment complexed with dansyl-lysine. Determined by X-ray diffraction at 1.85 Å resolution. Released 31 Jan 2006.

Method: X-ray diffraction
Resolution: 1.85 Å
Organism: Mus musculus
Chains: 2
Atoms: 1,884
Mol. weight: 26.76 kDa
Ligands: DNS
Released: 31 Jan 2006

Explore 1WZ1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1WZ1 contains 7 α-helices and 25 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 H: 3 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	4
β-strand	10-12	3	5
β-strand	18-25	8	4
α-helix	32	1
β-strand	33-40	8	5
β-strand	44-51	8	5
α-helix	54-56	3
β-strand	60-62	3	5
β-strand	70-75	6	4
β-strand	80-85	6	4
α-helix	90-92	3
β-strand	94-101	8	5
β-strand	102	1	6
β-strand	105	1	6
β-strand	115-119	5	5

Chain L: 4 helices, 13 β-strands

Element	Residues	Length	Sheet
α-helix	2-3	2
β-strand	4-7	4	1
β-strand	10-13	4	2
β-strand	19-25	7	1
β-strand	30	1	3
β-strand	36	1	3
β-strand	38-43	6	2
β-strand	50-54	5	2
β-strand	58-59	2	2
α-helix	60	1
β-strand	67-72	6	1
β-strand	75-80	6	1
α-helix	85-87	3
β-strand	89-95	7	2
α-helix	101	1
β-strand	102-103	2	2
β-strand	107-111	5	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ig light chain	L	protein	113	Mus musculus	P01631 (AlphaFold model)
Ig heavy chain	H	protein	123	Mus musculus

Sequence of entity 1 (L), FASTA

>1WZ1_1 Ig light chain (chains L)
DVVMTQTPLSLPVSLGNQASISCRSSQSLVHSNGNTYLHWYLQKPGQSPKLLIYKVSNRF
SGVPDRFSGSGSGTDFTLKISRVEAEDLGVYFCSQSTHVPFTFGSGTKLEIKR

Sequence of entity 2 (H), FASTA

>1WZ1_2 Ig heavy chain (chains H)
EVKLEESGGGLVQPGGSMKLSCATSGFTFSDAWMDWVRQSPEKGLEWVAEIRNKANNHAT
YYAESVKGRFTISRDDSKRRVYLQMNTLRAEDTGIYYCTGIYYHYPWFAYWGQGTLVTVS
AEP

Ligands and cofactors

ID	Name	Formula	Copies
DNS	N~6~-{[5-(dimethylamino)-1-naphthyl]sulfonyl}-L-lysine	C18 H25 N3 O4 S	1

Primary citation

Conformational dynamics of complementarity-determining region H3 of an anti-dansyl Fv fragment in the presence of its hapten. Nakasako, M., Oka, T., Mashumo, M. et al. J Mol Biol (2005) 351:627-640. DOI 10.1016/j.jmb.2005.06.018 · PubMed

Other PDB entries of the same protein (UniProt P01631 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1DLF 1.45 Å, High resolution crystal structure of the fv fragment from an anti-dansyl switch variant…
2DLF 1.55 Å, High resolution crystal structure of the fv fragment from an anti-dansyl switch variant…
1N4X 1.7 Å, Structure of scFv 1696 at acidic pH
1SVZ 1.89 Å, Crystal structure of the single-chain Fv fragment 1696 in complex with the epitope…
2IPT 2.0 Å, PFA1 Fab Fragment
2IQA 2.0 Å, PFA2 FAB fragment, monoclinic apo form
2HKF 2.01 Å, Crystal structure of the Complex Fab M75- Peptide
2O5X 2.05 Å, Crystal structure of 1E9 LeuH47Trp/ArgH100Trp, an engineered Diels-Alderase Fab with nM…
1BFV 2.1 Å, Monoclonal antibody fragment FV4155 from E. Coli
1CFV 2.1 Å, Monoclonal antibody fragment FV4155 from E. Coli
2HKH 2.1 Å, Crystal structure of the Fab M75
2O5Z 2.4 Å, Crystal structure of the 1E9 LeuH47Trp/ArgH100Trp Fab 5-beta-androstane-3,17-dione complex

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