28MS: Serotransferrin

X-ray structure of the adduct between human serum transferrin with Fe3+ bound at the C-lobe and dirhodium tetraacetate. Determined by X-ray diffraction at 2.37 Å resolution. Released 11 Mar 2026.

Method: X-ray diffraction
Resolution: 2.37 Å
Organism: Homo sapiens
Chains: 1
Atoms: 5,643
Mol. weight: 80.21 kDa
Ligands: FE, MLI, A1JZ3
Released: 11 Mar 2026

Explore 28MS in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

28MS contains 38 α-helices and 32 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: 38 helices, 32 β-strands

Element	Residues	Length	Sheet
β-strand	5-10	6	1
α-helix	13-26	14
β-strand	36-41	6	1
α-helix	45-53	9
β-strand	59	1	1
β-strand	60-62	3	2
α-helix	64-71	8
β-strand	77-84	8	2
β-strand	85	1	3
β-strand	92	1	3
β-strand	94-102	9	4
α-helix	109-111	3
β-strand	116-119	4	4
α-helix	125-129	5
α-helix	130-134	5
α-helix	136-138	3
α-helix	140	1
α-helix	142	1
α-helix	146-151	6
β-strand	156-158	3	4
α-helix	168-171	4
α-helix	187-196	10
β-strand	202-206	5	4
α-helix	209-213	5
α-helix	217-220	4
β-strand	223-226	4	4
β-strand	232-234	3	4
α-helix	238-240	3
β-strand	244-247	4	4
β-strand	250-254	5	2
α-helix	260-274	15
β-strand	301-304	4	2
α-helix	305-306	2
α-helix	311-315	5
α-helix	317-328	12
β-strand	342-346	5	5
α-helix	350-362	13
β-strand	366-370	5	5
α-helix	374-383	10
β-strand	388	1	5
β-strand	389-391	3	6
α-helix	393-401	9
β-strand	405-411	7	6
β-strand	427-433	7	7
β-strand	440	1	8
β-strand	443	1	8
β-strand	449-451	3	7
α-helix	457-461	5
α-helix	462-471	10
α-helix	476-478	3
β-strand	483-484	2	7
α-helix	493-495	3
α-helix	502-504	3
α-helix	516-526	11
β-strand	530-534	5	7
α-helix	537-540	4
α-helix	549-552	4
α-helix	556-558	3
β-strand	559-562	4	7
β-strand	568-570	3	7
α-helix	574-576	3
β-strand	580-581	2	7
α-helix	583-585	3
β-strand	586-589	4	6
α-helix	591-593	3
α-helix	594-608	15
β-strand	637-640	4	6
α-helix	647-651	5
α-helix	653-663	11
α-helix	669-677	9

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Serotransferrin	A	protein	679	Homo sapiens	P02787 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>28MS_1 Serotransferrin (chains A)
VPDKTVRWCAVSEHEATKCQSFRDHMKSVIPSDGPSVACVKKASYLDCIRAIAANEADAV
TLDAGLVYDAYLAPNNLKPVVAEFYGSKEDPQTFYYAVAVVKKDSGFQMNQLRGKKSCHT
GLGRSAGWNIPIGLLYCDLPEPRKPLEKAVANFFSGSCAPCADGTDFPQLCQLCPGCGCS
TLNQYFGYSGAFKCLKDGAGDVAFVKHSTIFENLANKADRDQYELLCLDNTRKPVDEYKD
CHLAQVPSHTVVARSMGGKEDLIWELLNQAQEHFGKDKSKEFQLFSSPHGKDLLFKDSAH
GFLKVPPRMDAKMYLGYEYVTAIRNLREGTCPEAPTDECKPVKWCALSHHERLKCDEWSV
NSVGKIECVSAETTEDCIAKIMNGEADAMSLDGGFVYIAGKCGLVPVLAENYNKSDNCED
TPEAGYFAVAVVKKSASDLTWDNLKGKKSCHTAVGRTAGWNIPMGLLYNKINHCRFDEFF
SEGCAPGSKKDSSLCKLCMGSGLNLCEPNNKEGYYGYTGAFRCLVEKGDVAFVKHQTVPQ
NTGGKNPDPWAKNLNEKDYELLCLDGTRKPVEEYANCHLARAPNHAVVTRKDKEACVHKI
LRQQQHLFGSNVTDCSGNFCLFRSETKDLLFRDDTVCLAKLHDRNTYEKYLGEEYVKAVG
NLRKCSTSSLLEACTFRRP

Ligands and cofactors

ID	Name	Formula	Copies
FE	FE (III) ion	Fe	1
MLI	Malonate ion	C3 H2 O4	1
A1JZ3	Rhodium tetraacetate dihydrate	C8 H14 O10 Rh2	9

Water and common crystallization additives (ACT, PEG, GOL) are not listed.

Primary citation

Ru and Rh binding sites in the structure of human serum transferrin with Fe 3+ bound at the C-lobe. Banneville, A.S., Ferraro, G., D'Elia, R. et al. Dalton Trans (2026) 55:4051-4056. DOI 10.1039/d6dt00205f · PubMed

Other PDB entries of the same protein (UniProt P02787 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1RYO 1.2 Å, Human serum transferrin, N-lobe bound with oxalate
1A8E 1.6 Å, Human serum transferrin, recombinant N-terminal lobe
3SKP 1.7 Å, The structure of apo-human transferrin C-lobe with bound sulfate ions
1A8F 1.8 Å, Human serum transferrin, recombinant N-terminal lobe
1D3K 1.8 Å, Human serum transferrin
1FQE 1.8 Å, Crystal structures of mutant (K206A) that abolish the dilysine interaction in the N-lobe…
3FGS 1.8 Å, Crystal structure of G65R/K206E double mutant of the N-lobe human transferrin
1JQF 1.85 Å, Human Transferrin N-Lobe Mutant H249Q
1OQG 1.9 Å, Crystal structure of the D63E mutant of the N-lobe human transferrin
9RTB 1.93 Å, Crystal structure of the adduct formed upon reaction of [V(IV)O(acetylacetonate)2] with…
1D4N 2.0 Å, Human serum transferrin
1N84 2.05 Å, Human serum transferrin, N-lobe

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