3BSZ: Transthyretin

Crystal structure of the transthyretin-retinol binding protein-Fab complex. Determined by X-ray diffraction at 3.38 Å resolution. Released 11 Nov 2008.

Method: X-ray diffraction
Resolution: 3.38 Å
Organisms: Homo sapiens, Mus musculus
Chains: 10
Atoms: 13,428
Mol. weight: 189.43 kDa
Ligands: RTL
Released: 11 Nov 2008

Explore 3BSZ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3BSZ contains 29 α-helices and 166 β-strands across 10 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.

Chains A and C: 1 helix, 12 β-strands

Element	Residues	Length	Sheet
β-strand	12-16	5	1
β-strand	17-18	2	2
β-strand	23-24	2	2
β-strand	29-35	7	3
β-strand	41-48	8	3
β-strand	67-73	7	3
α-helix	76-82	7
β-strand	88	1	4
β-strand	91-97	7	3
β-strand	104-109	6	1
β-strand	112	1	1
β-strand	115-116	2	1
β-strand	119-123	5	1

Chains B and D: 1 helix, 11 β-strands

Element	Residues	Length	Sheet
β-strand	12-18	7	1
β-strand	23-24	2	1
β-strand	29-35	7	4
β-strand	41-48	8	4
β-strand	54-55	2	1
β-strand	67-73	7	4
α-helix	75-81	7
β-strand	84	1	5
β-strand	88	1	3
β-strand	91-97	7	4
β-strand	105-112	8	1
β-strand	115-121	7	1

Chain E: 5 helices, 12 β-strands

Element	Residues	Length	Sheet
α-helix	11-12	2
α-helix	17-20	4
β-strand	22-30	9	11
β-strand	42-47	6	11
β-strand	53-61	9	11
β-strand	69-80	12	11
β-strand	82-92	11	11
β-strand	97	1	5
β-strand	100-109	10	11
β-strand	114-120	7	11
β-strand	123	1	12
β-strand	129	1	12
β-strand	132-138	7	11
α-helix	146-158	13
α-helix	165	1
β-strand	166-167	2	11
α-helix	168	1

Chain F: 5 helices, 12 β-strands

Element	Residues	Length	Sheet
α-helix	11-12	2
α-helix	17-20	4
β-strand	22-30	9	13
β-strand	42-47	6	13
β-strand	53-61	9	13
β-strand	69-80	12	13
β-strand	82-92	11	13
β-strand	97	1	10
β-strand	100-109	10	13
β-strand	114-119	6	13
β-strand	123	1	14
β-strand	129	1	14
β-strand	133-138	6	13
α-helix	146-158	13
α-helix	165	1
β-strand	166-167	2	13
α-helix	168	1

Chains H and N: 3 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	3-4	2	21
α-helix	7-9	3
β-strand	10-11	2	22
β-strand	18-20	3	23
β-strand	23	1	23
β-strand	24-25	2	21
β-strand	32	1	24
β-strand	35-39	5	25
β-strand	46-52	7	25
β-strand	57-60	4	25
β-strand	68-73	6	23
β-strand	78-83	6	23
β-strand	93-98	6	25
β-strand	100	1	24
β-strand	107-108	2	25
β-strand	112	1	25
β-strand	114-115	2	22
β-strand	122	1	26
β-strand	126-129	4	27
β-strand	141-150	10	27
β-strand	151	1	26
β-strand	157-159	3	28
α-helix	160-162	3
β-strand	168-171	4	27
β-strand	180-188	9	27
β-strand	200-204	5	28
α-helix	205-207	3
β-strand	209-213	5	28

Chain L: 4 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	4-5	2	15
β-strand	10-14	5	16
β-strand	19-25	7	15
β-strand	37-42	6	16
β-strand	50-53	4	16
β-strand	57-58	2	16
β-strand	60	1	17
β-strand	62	1	17
β-strand	68-71	4	15
β-strand	74-79	6	15
α-helix	84-86	3
β-strand	89-94	6	16
α-helix	100	1
β-strand	101-102	2	16
β-strand	107-111	5	16
β-strand	115	1	18
β-strand	118-122	5	19
α-helix	126-129	4
β-strand	134-141	8	19
β-strand	144	1	18
β-strand	149-154	6	20
β-strand	157-159	3	20
β-strand	163	1	19
β-strand	167-168	2	19
β-strand	178-185	8	19
β-strand	195-201	7	20
α-helix	208	1
β-strand	209-214	6	20

Chain M: 5 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	4-5	2	29
β-strand	10-14	5	30
β-strand	21-25	5	29
β-strand	37-42	6	30
β-strand	50-53	4	30
β-strand	57-58	2	30
β-strand	68-71	4	29
β-strand	74-77	4	29
α-helix	84-86	3
β-strand	89-94	6	30
α-helix	100	1
β-strand	101-102	2	30
β-strand	107-111	5	30
β-strand	115	1	31
β-strand	118-122	5	32
α-helix	126-129	4
β-strand	134-141	8	32
β-strand	144	1	31
β-strand	149-154	6	33
β-strand	157-159	3	33
β-strand	163	1	32
β-strand	166-168	3	32
β-strand	178-185	8	32
α-helix	188-190	3
β-strand	195-201	7	33
α-helix	208	1
β-strand	209-214	6	33

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Transthyretin	A, B, C, D	protein	127	Homo sapiens	P02766 (AlphaFold model)
Plasma retinol-binding protein	E, F	protein	176	Homo sapiens	P02753 (AlphaFold model)
Fab fragment heavy chain	L, M	protein	215	Mus musculus	P01660 (AlphaFold model), P01837 (AlphaFold model)
Fab fragment light chain	H, N	protein	215	Mus musculus

Sequence of entity 1 (A, B, C, D), FASTA

>3BSZ_1 Transthyretin (chains A, B, C, D)
GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTT
EEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTA
VVTNPKE

Sequence of entity 2 (E, F), FASTA

>3BSZ_2 Plasma retinol-binding protein (chains E, F)
ERDCRVSSFRVKENFDKARFSGTWYAMAKKDPEGLFLQDNIVAEFSVDETGQMSATAKGR
VRLLNNWDVCADMVGTFTDTEDPAKFKMKYWGVASFLQKGNDDHWIVDTDYDTYAVQYSC
RLLNLDGTCADSYSFVFSRDPNGLPPEAQKIVRQRQEELCLARQYRLIVHNGYCDG

Sequence of entity 3 (L, M), FASTA

>3BSZ_3 Fab fragment heavy chain (chains L, M)
DIVLTQSPSSLAVSLGQRATISCRASESVDSYGNSFMHWYQQKPGQPPKLLIYRASNLES
GIPARFSGSGSRTDFTLTINPVEADDVATYYCQQSNEDPYTFGGGTKLEIKRADAAPTVS
IFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMS
STLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNR

Sequence of entity 4 (H, N), FASTA

>3BSZ_4 Fab fragment light chain (chains H, N)
DVQLQESGTVLARPGASVKMSCKASGYSFTSYWMHWIKQRPGQGLEWIGGVYPGDSHTSY
NQKFKGKAKLTAVTSASTAYMELSSLTNEDSAVYYCTRSGFDYGNEDWGQGTTLTVSSAK
TTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSDLY
TLSSSVTVPSSPRPSETVTCNVAHPASSTKVDKKI

Ligands and cofactors

ID	Name	Formula	Copies
RTL	Retinol	C20 H30 O	2

Primary citation

Structural and mutational analyses of protein-protein interactions between transthyretin and retinol-binding protein. Zanotti, G., Folli, C., Cendron, L. et al. FEBS J (2008) 275:5841-5854. DOI 10.1111/j.1742-4658.2008.06705.x · PubMed

Other PDB entries of the same protein (UniProt P02766 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1F86 1.1 Å, Transthyretin THR119MET protein stabilisation
8C86 1.1 Å, Crystal structure of human transthyretin in complex with 3-O-methyltolcapone analogue 2
8W45 1.1 Å, X-ray crystal structure of V30M-TTR in complex with pinostilbene
4QXV 1.12 Å, Crystal structure of human transthyretin in complex with luteolin at 1.1 a resolution
4KY2 1.13 Å, Transthyretin in complex with the fluorescent folding sensor…
4D7B 1.15 Å, Structure of human transthyretin in complex with Tolcapone
7EJQ 1.15 Å, Crystal structure of human transthyretin in complex with…
8AWI 1.15 Å, Crystal structure of Human Transthyretin at 1.15 Angstrom resolution
6TXW 1.15 Å, V30G Transthyretin structure in complex with Tolcalpone
4L1T 1.16 Å, Transthyretin in complex with (E)-3-(dimethylamino)-5-(4-hydroxy-3,5-dimethylstyryl)benzo…
4HIQ 1.18 Å, The Structure of V122I Mutant Transthyretin in Complex with AG10
9H7L 1.18 Å, Human Transthyretin in Complex with 4-phenyl-1H-pyrazolo[3,4-b]pyridin-3-amine

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