1IEJ: Ovotransferrin, N-terminal lobe, holo form

Ovotransferrin, N-terminal lobe, holo form, at 1.65 a resolution. Determined by X-ray diffraction at 1.65 Å resolution. Released 20 Jun 2001.

Method: X-ray diffraction
Resolution: 1.65 Å
Organism: Gallus gallus
Chains: 1
Atoms: 2,827
Mol. weight: 36.66 kDa
Ligands: FE, CO3
Released: 20 Jun 2001

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

Secondary structure: helices and β-sheets

1IEJ contains 19 α-helices and 15 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, 15 β-strands

Element	Residues	Length	Sheet
β-strand	5-11	7	1
α-helix	14-26	13
β-strand	32-38	7	1
α-helix	42-50	9
β-strand	56	1	1
β-strand	57-59	3	2
α-helix	61-67	7
β-strand	75-83	9	2
β-strand	88-89	2	2
β-strand	91-99	9	3
α-helix	106-108	3
β-strand	113-116	4	3
α-helix	122-126	5
α-helix	127-134	8
α-helix	143-145	3
α-helix	148-155	8
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	236-238	3
β-strand	245-248	4	3
α-helix	249-250	2
β-strand	251-254	4	2
α-helix	260-274	15
α-helix	293-295	3
β-strand	304-309	6	2
α-helix	310-311	2
α-helix	316-320	5
α-helix	322-331	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ovotransferrin	A	protein	332	Gallus gallus	P02789 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1IEJ_1 OVOTRANSFERRIN (chains A)
APPKSVIRWCTISSPEEKKCNNLRDLTQQERISLTCVQKATYLDCIKAIANNEADAITLD
GGQVFEAGLAPYKLKPIAAEVYEHTEGSTTSYYAVAVVKKGTEFTVNDLQGKTSCHTGLG
RSAGWNIPIGTLLHRGAIEWEGIESGSVEQAVAKFFSASCVPGATIEQKLCRQCKGDPKT
KCARNAPYSGYSGAFHCLKDGKGDVAFVKHTTVNENAPDQKDEYELLCLDGSRQPVDNYK
TCNWARVAAHAVVARDDNKVEDIWSFLSKAQSDFGVDTKSDFHLFGPPGKKDPVLKDLLF
KDSAIMLKRVPSLMDSQLYLGFEYYSAIQSMR

Ligands and cofactors

ID	Name	Formula	Copies
FE	FE (III) ion	Fe	1
CO3	Carbonate ion	C O3	1

Primary citation

Domain closure mechanism in transferrins: new viewpoints about the hinge structure and motion as deduced from high resolution crystal structures of ovotransferrin N-lobe. Mizutani, K., Mikami, B., Hirose, M. J Mol Biol (2001) 309:937-947. DOI 10.1006/jmbi.2001.4719 · 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…
1TFA 1.9 Å, Ovotransferrin, N-terminal lobe, apo form
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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