2BFV: Monoclonal antibody fragment FV4155 from E. Coli

Monoclonal antibody fragment FV4155 from E. Coli. Determined by X-ray diffraction at 2.5 Å resolution. Released 3 Dec 1997.

Method: X-ray diffraction
Resolution: 2.5 Å
Organism: Mus musculus
Chains: 2
Atoms: 1,877
Mol. weight: 26.09 kDa
Ligands: STG
Released: 3 Dec 1997

Explore 2BFV in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2BFV contains 6 α-helices and 22 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: 2 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	3
β-strand	10-13	4	4
β-strand	18-25	8	3
α-helix	29-31	3
β-strand	33-39	7	4
β-strand	45-51	7	4
β-strand	57-59	3	4
β-strand	68-73	6	3
β-strand	78-83	6	3
α-helix	88-90	3
β-strand	92-100	9	4
β-strand	105-109	5	4
β-strand	113-118	6	4

Chain L: 4 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	1
β-strand	10-13	4	2
β-strand	19-25	7	1
β-strand	38-43	6	2
α-helix	48-49	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	90-95	6	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
FV4155	L	protein	113	Mus musculus	P01631 (AlphaFold model)
FV4155	H	protein	119	Mus musculus

Sequence of entity 1 (L), FASTA

>2BFV_1 FV4155 (chains L)
DIELTQSPPSLPVSLGDQVSISCRSSQSLVSNNRRNYLHWYLQKPGQSPKLVIYKVSNRF
SGVPDRFSGSGSGTDFTLKISRVAAEDLGLYFCSQSSHVPLTFGSGTKLEIKR

Sequence of entity 2 (H), FASTA

>2BFV_2 FV4155 (chains H)
QVQLQESGGGLVNLGGSMTLSCVASGFTFNTYYMSWVRQTPEKTLELVAAINSDGEPIYY
PDTLKGRVTISRDNAKKTLYLQMSSLNFEDTALYYCARLNYAVYGMDYWGQGTTVTVSS

Ligands and cofactors

ID	Name	Formula	Copies
STG	Estriol 3-(B-D-glucuronide)	C24 H32 O9	1

Primary citation

Antibody fragment Fv4155 bound to two closely related steroid hormones: the structural basis of fine specificity. Trinh, C.H., Hemmington, S.D., Verhoeyen, M.E. et al. Structure (1997) 5:937-948. DOI 10.1016/S0969-2126(97)00247-5 · 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
1WZ1 1.85 Å, Crystal structure of the Fv fragment complexed with dansyl-lysine
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

Browse structure collections

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