1IQ7: Ovotransferrin, C-Terminal Lobe, Apo Form

Ovotransferrin, C-Terminal Lobe, Apo Form. Determined by X-ray diffraction at 2.3 Å resolution. Released 28 Nov 2001.

Method: X-ray diffraction
Resolution: 2.3 Å
Organism: Gallus gallus
Chains: 1
Atoms: 2,713
Mol. weight: 38.74 kDa
Ligands: NAG
Released: 28 Nov 2001

Explore 1IQ7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1IQ7 contains 18 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: 18 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	346-350	5	1
α-helix	351-364	14
β-strand	370-374	5	1
α-helix	377-385	9
β-strand	391	1	1
β-strand	392-394	3	2
α-helix	396-404	9
β-strand	408-414	7	2
β-strand	429-438	10	3
β-strand	452-455	4	3
α-helix	461-465	5
α-helix	466-475	10
α-helix	480-483	4
β-strand	486-488	3	3
α-helix	497-500	4
α-helix	523-533	11
β-strand	537-541	5	3
α-helix	544-547	4
α-helix	563-565	3
β-strand	566-569	4	3
β-strand	575-577	3	3
α-helix	578-583	6
β-strand	587-590	4	3
α-helix	591-592	2
β-strand	593-596	4	2
α-helix	598-600	3
α-helix	601-615	15
β-strand	643-646	4	2
α-helix	647	1
α-helix	653-657	5
α-helix	659-670	12
α-helix	675-683	9

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ovotransferrin	A	protein	345	Gallus gallus	P02789 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1IQ7_1 Ovotransferrin (chains A)
ENRIQWCAVGKDEKSKCDRWSVVSNGDVECTVVDETKDCIIKIMKGEADAVALDGGLVYT
AGVCGLVPVMAERYDDESQCSKTDERPASYFAVAVARKDSNVNWNNLKGKKSCHTAVGRT
AGWVIPMGLIHNRTGTCNFDEYFSEGCAPGSPPNSRLCQLCQGSGGIPPEKCVASSHEKY
FGYTGALRCLVEKGDVAFIQHSTVEENTGGKNKADWAKNLQMDDFELLCTDGRRANVMDY
RECNLAEVPTHAVVVRPEKANKIRDLLERQEKRFGVNGSEKSKFMMFESQNKDLLFKDLT
KCLFKVREGTTYKEFLGDKFYTVISSLKTCNPSDILQMCSFLEGK

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	1

Water and common crystallization additives (SO4) are not listed.

Primary citation

Anion-mediated Fe3+ release mechanism in ovotransferrin C-lobe: a structurally identified SO4(2-) binding site and its implications for the kinetic pathway. Mizutani, K., Muralidhara, B.K., Yamashita, H. et al. J Biol Chem (2001) 276:35940-35946. DOI 10.1074/jbc.M102590200 · 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
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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