1TFA: Ovotransferrin, N-terminal lobe, apo form

Ovotransferrin, N-terminal lobe, apo form. Determined by X-ray diffraction at 1.9 Å resolution. Released 13 Jan 1999.

Method: X-ray diffraction
Resolution: 1.9 Å
Organism: Gallus gallus
Chains: 1
Atoms: 2,844
Mol. weight: 36.63 kDa
Released: 13 Jan 1999

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

Secondary structure: helices and β-sheets

1TFA contains 19 α-helices and 14 β-strands across 1 chain. 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: 19 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	6-11	6	1
α-helix	14-27	14
β-strand	33-38	6	1
α-helix	42-50	9
β-strand	56	1	1
β-strand	57-59	3	2
α-helix	61-68	8
β-strand	74-81	8	2
α-helix	83-85	3
β-strand	90-99	10	3
α-helix	106-108	3
β-strand	113-116	4	3
α-helix	122-126	5
α-helix	127-134	8
α-helix	148-153	6
β-strand	158-160	3	3
α-helix	168-171	4
α-helix	190-199	10
β-strand	205-209	5	3
α-helix	212-216	5
α-helix	221-223	3
β-strand	224-227	4	3
β-strand	233-235	3	3
α-helix	236-241	6
β-strand	245-248	4	3
α-helix	249-250	2
β-strand	251-255	5	2
α-helix	260-274	15
α-helix	293-295	3
β-strand	306-309	4	2
α-helix	310-311	2
α-helix	316-320	5
α-helix	322-329	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein (ovotransferrin)	A	protein	329	Gallus gallus	P02789 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1TFA_1 PROTEIN (OVOTRANSFERRIN) (chains A)
KSVIRWCTVSSPEEKKCNNLRDLTQQERISLTCVQKATYLDCIKAIANNEADAISLDGGQ
VFEAGLAPYKLKPIAAEVYEHTEGSTTSYYAVAVVKKGTEFTVNDLQGKTSCHTGLGRSA
GWNIPIGTLIHRGAIEWEGIESGSVEQAVAKFFSASCVPGATIEQKLCRQCKGDPKTKCA
RNAPYSGYSGAFHCLKDGKGDVAFVKHTTVNENAPDQKDEYELLCLDGSRQPVDNYKTCN
WARVAAHAVVARDDNKVEDIWSFLSKAQSDFGVDTKSDFHLFGPPGKKDPVLKDLLFKDS
AIMLKRVPSLMDSQLYLGFEYYSAIQSMR

Primary citation

Alternative structural state of transferrin. The crystallographic analysis of iron-loaded but domain-opened ovotransferrin N-lobe. Mizutani, K., Yamashita, H., Kurokawa, H. et al. J Biol Chem (1999) 274:10190-10194. DOI 10.1074/jbc.274.15.10190 · PubMed

Other PDB entries of the same protein (UniProt P02789 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8X3H 0.93 Å, Crystal structure of iron-bound recombinant ovotransferrin N-lobe at 0.93 angstrom…
1IEJ 1.65 Å, Ovotransferrin, N-terminal lobe, holo form, at 1.65 a resolution
1NFT 2.1 Å, Ovotransferrin, N-terminal lobe, iron loaded open form
2D3I 2.15 Å, Crystal Structure of Aluminum-Bound Ovotransferrin at 2.15 Angstrom Resolution
1IQ7 2.3 Å, Ovotransferrin, C-Terminal Lobe, Apo Form
1NNT 2.3 Å, Structural evidence for a PH-sensitive di-lysine trigger in the hen ovotransferrin…
1OVT 2.4 Å, Refined crystallographic structure of hen ovotransferrin at 2.4 Å resolution
1N04 2.8 Å, Diferric chicken serum transferrin at 2.8 A resolution.
1AIV 3.0 Å, Apo ovotransferrin
8FEI 3.0 Å, CryoEM structure of Conalbumin from chicken egg white (sigma-Cas 1391-06-6)
1D9K 3.2 Å, Crystal structure of complex between D10 TCR and pmhc I-ak/ca
1RYX 3.5 Å, Crystal structure of hen serum transferrin in apo- form

Browse structure collections

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