1T66: FAB with intermediate affinity for fluorescein

The structure of FAB with intermediate affinity for fluorescein. Determined by X-ray diffraction at 2.3 Å resolution. Released 18 May 2004.

Method: X-ray diffraction
Resolution: 2.3 Å
Organism: Mus musculus
Chains: 4
Atoms: 7,005
Mol. weight: 97.05 kDa
Ligands: FLU
Released: 18 May 2004

Explore 1T66 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1T66 contains 26 α-helices and 89 β-strands across 4 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 C: 5 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	12
β-strand	10-13	4	13
β-strand	19-25	7	12
β-strand	30	1	14
β-strand	36	1	14
β-strand	38-43	6	13
β-strand	50-54	5	13
α-helix	55-57	3
β-strand	58-59	2	13
β-strand	67-72	6	12
β-strand	75-80	6	12
α-helix	85-87	3
β-strand	89-95	7	13
β-strand	102-103	2	13
β-strand	107-111	5	13
β-strand	116	1	15
α-helix	117-118	2
β-strand	119-123	5	16
α-helix	127-131	5
β-strand	134-144	11	16
β-strand	145	1	15
β-strand	149-155	7	17
β-strand	158-159	2	17
β-strand	164-168	5	16
β-strand	178-187	10	16
α-helix	188-191	4
β-strand	196-203	8	17
β-strand	210-215	6	17

Chain D: 6 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	18
β-strand	10-12	3	19
β-strand	18-25	8	18
α-helix	29-31	3
β-strand	33-40	8	19
β-strand	44-51	8	19
β-strand	60-62	3	19
β-strand	70-75	6	18
β-strand	80-85	6	18
α-helix	90-92	3
β-strand	94-101	8	19
β-strand	106-108	3	19
β-strand	112-116	5	19
α-helix	120-121	2
β-strand	122	1	20
β-strand	125-129	5	21
β-strand	140-150	11	21
β-strand	151	1	20
β-strand	156-159	4	22
α-helix	160-162	3
β-strand	164	1	22
β-strand	168-170	3	21
α-helix	171-173	3
β-strand	174-175	2	21
β-strand	180-189	10	21
β-strand	199-204	6	22
α-helix	205-207	3
β-strand	209-214	6	22

Chain H: 6 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	7
β-strand	10-12	3	8
β-strand	18-25	8	7
α-helix	29-31	3
β-strand	33-40	8	8
β-strand	44-51	8	8
α-helix	54-56	3
β-strand	60-62	3	8
β-strand	70-75	6	7
β-strand	80-85	6	7
α-helix	90-92	3
β-strand	94-101	8	8
β-strand	106-108	3	8
β-strand	112-116	5	8
β-strand	122	1	9
β-strand	125-129	5	10
β-strand	142-150	9	10
β-strand	151	1	9
β-strand	156-159	4	11
α-helix	160-162	3
β-strand	168-170	3	10
α-helix	171-173	3
β-strand	174-176	3	10
β-strand	179-187	9	10
β-strand	199-204	6	11
α-helix	205-207	3
β-strand	209-214	6	11

Chain L: 9 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	1
β-strand	10-14	5	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	49-54	6	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	107-112	6	2
β-strand	116	1	4
β-strand	119-123	5	5
α-helix	124-126	3
α-helix	127-132	6
β-strand	134-144	11	5
β-strand	145	1	4
β-strand	150-155	6	6
β-strand	158-159	2	6
α-helix	160	1
β-strand	164-168	5	5
α-helix	169-172	4
β-strand	178-187	10	5
α-helix	188-191	4
β-strand	196-202	7	6
α-helix	209	1
β-strand	210-215	6	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
immunoglobulin light chain	C, L	protein	219	Mus musculus	Q65ZC0 (AlphaFold model)
immunoglobulin heavy chain	D, H	protein	220	Mus musculus	Q91Z05 (AlphaFold model)

Sequence of entity 1 (C, L), FASTA

>1T66_1 immunoglobulin light chain (chains C, L)
DVVMTQTPLSLPVSLGDQASISCRSSQSLVHSNGNTYLHWYLQKPGQSPKLLIYKVSNRF
SGVPDRFSGSGSGTDFTLKISRVEAEDLGVYFCSQSTHVPWTFGGGTKLEIKRADAAPTV
SIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQNSKDSTYSM
SSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC

Sequence of entity 2 (D, H), FASTA

>1T66_2 immunoglobulin heavy chain (chains D, H)
EVKLDETGGGLVQPGRPMKLSCVASGFTFSDYWMNWVRQSPEKGLEWVAQIRNKPYNYET
YYSDSVKGRFTISRDDSKSSVYLQMNNLRAEDMGIYYCTSYGYHGAYWGQGTLVTVSAAK
TTAPSVYPLAPGTAALKSSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSALY
TLTSSVTVPSSSWPSQTVTCNVAHPASSTKVDKKIVPRNC

Ligands and cofactors

ID	Name	Formula	Copies
FLU	2-(6-hydroxy-3-oxo-3H-xanthen-9-yl)-benzoic acid	C20 H12 O5	2

Primary citation

Three-dimensional Structures of Idiotypically Related Fabs with Intermediate and High Affinity for Fluorescein. Terzyan, S., Ramsland, P.A., Voss Jr., E.W. et al. J Mol Biol (2004) 339:1141-1151. DOI 10.1016/j.jmb.2004.03.080 · PubMed

Other PDB entries of the same protein (UniProt Q65ZC0 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2G60 1.85 Å, Structure of anti-FLAG M2 Fab domain
1LO2 2.0 Å, Retro-Diels-Alderase Catalytic Antibody
1L7T 2.1 Å, Crystal Structure Analysis of the anti-testosterone Fab fragment
1LO3 2.3 Å, Retro-Diels-Alderase Catalytic Antibody: Product Analogue
1LO4 2.4 Å, Retro-Diels-Alderase Catalytic antibody 9D9
2GK0 2.45 Å, Structure of Catalytic Elimination Antibody 13G5 from a twinned crystal in space group C2
1I9J 2.6 Å, Testosterone complex structure of the recombinant monoclonal wild type anti-testosterone…
2GJZ 2.65 Å, Structure of Catalytic Elimination Antibody 13G5 from a crystal in space group P2(1)
1I9I 2.72 Å, Native crystal structure of the recombinant monoclonal wild type anti-testosterone FAB…

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