1AIV: Apo ovotransferrin

Apo ovotransferrin. Determined by X-ray diffraction at 3.0 Å resolution. Released 29 Apr 1998.

Method: X-ray diffraction
Resolution: 3.0 Å
Organism: Gallus gallus
Chains: 1
Atoms: 5,340
Mol. weight: 76.35 kDa
Released: 29 Apr 1998

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

Secondary structure: helices and β-sheets

1AIV contains 26 α-helices and 36 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: 26 helices, 36 β-strands

Element	Residues	Length	Sheet
β-strand	6-7	2	1
β-strand	9	1	2
α-helix	14-29	16
β-strand	33-34	2	1
α-helix	42-48	7
α-helix	49-53	5
β-strand	56	1	2
β-strand	58-59	2	3
α-helix	61-68	8
β-strand	78-81	4	4
β-strand	94	1	5
β-strand	97-99	3	6
α-helix	126-134	9
α-helix	150-153	4
β-strand	160	1	7
β-strand	171	1	7
α-helix	195-199	5
β-strand	209	1	5
α-helix	212-215	4
β-strand	224-227	4	6
β-strand	233-234	2	6
β-strand	245	1	5
β-strand	251-252	2	3
α-helix	261-272	12
α-helix	293-295	3
β-strand	306-309	4	4
α-helix	316-319	4
α-helix	322-329	8
β-strand	345	1	8
β-strand	348-350	3	9
α-helix	352-362	11
β-strand	369	1	8
β-strand	372-374	3	9
α-helix	379-385	7
β-strand	393-394	2	10
α-helix	396-405	10
β-strand	408-411	4	10
β-strand	414	1	11
α-helix	418-420	3
β-strand	432-438	7	12
β-strand	452-455	4	12
α-helix	461-465	5
α-helix	466-472	7
β-strand	486-488	3	12
β-strand	490	1	13
β-strand	492	1	13
α-helix	524-533	10
β-strand	537-541	5	12
α-helix	542-544	3
β-strand	566-568	3	12
β-strand	577	1	12
α-helix	581-584	4
β-strand	587-588	2	12
α-helix	589-591	3
β-strand	593-596	4	10
α-helix	601-614	14
β-strand	635	1	14
β-strand	637	1	14
β-strand	643	1	11
α-helix	653-657	5
α-helix	659-669	11
α-helix	675-684	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ovotransferrin	A	protein	686	Gallus gallus	P02789 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1AIV_1 OVOTRANSFERRIN (chains A)
APPKSVIRWCTISSPEEKKCNNLRDLTQQERISLTCVQKATYLDCIKAIANNEADAISLD
GGQAFEAGLAPYKLKPIAAEVYEHTEGSTTSYYAVAVVKKGTEFTVNDLQGKTSCHTGLG
RSAGWNIPIGTLLHRGAIEWEGIESGSVEQAVAKFFSASCVPGATIEQKLCRQCKGDPKT
KCARNAPYSGYSGAFHCLKDGKGDVAFVKHTTVNENAPDQKDEYELLCLDGSRQPVDNYK
TCNWARVAAHAVVARDDNKVEDIWSFLSKAQSDFGVDTKSDFHLFGPPGKKDPVLKDLLF
KDSAIMLKRVPSLMDSQLYLGFEYYSAIQSMRKDQLTPSPRENRIQWCAVGKDEKSKCDR
WSVVSNGDVECTVVDETKDCIIKIMKGEADAVALDGGLVYTAGVCGLVPVMAERYDDESQ
CSKTDERPASYFAVAVARKDSNVNWNNLKGKKSCHTAVGRTAGWVIPMGLIHNRTGTCNF
DEYFSEGCAPGSPPNSRLCQLCQGSGGIPPEKCVASSHEKYFGYTGALRCLVEKGDVAFI
QHSTVEENTGGKNKADWAKNLQMDDFELLCTDGRRANVMDYRECNLAEVPTHAVVVRPEK
ANKIRDLLERQEKRFGVNGSEKSKFMMFESQNKDLLFKDLTKCLFKVREGTTYKEFLGDK
FYTVISSLKTCNPSDILQMCSFLEGK

Primary citation

Crystal structure of hen apo-ovotransferrin. Both lobes adopt an open conformation upon loss of iron. Kurokawa, H., Dewan, J.C., Mikami, B. et al. J Biol Chem (1999) 274:28445-28452. DOI 10.1074/jbc.274.40.28445 · 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
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.
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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