6WBV: Human ferroportin

Structure of human ferroportin bound to hepcidin and cobalt in lipid nanodisc. Determined by electron microscopy at 2.5 Å resolution. Released 9 Sept 2020.

Method: Electron microscopy
Resolution: 2.5 Å
Organisms: Homo sapiens, Mus musculus
Chains: 4
Atoms: 6,860
Mol. weight: 118.04 kDa
Ligands: CO, AGA
Released: 9 Sept 2020

Explore 6WBV in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6WBV contains 33 α-helices and 47 β-strands across 4 chains. 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: 20 helices, 0 β-strands

Element	Residues	Length
α-helix	17-20	4
α-helix	24-53	30
α-helix	59-85	27
α-helix	88-115	28
α-helix	117-122	6
α-helix	126-153	28
α-helix	154-158	5
α-helix	159-162	4
α-helix	167-198	32
α-helix	201-229	29
α-helix	231-234	4
α-helix	290-303	14
α-helix	308-316	9
α-helix	328-334	7
α-helix	339-366	28
α-helix	369-390	22
α-helix	453-483	31
α-helix	486-488	3
α-helix	489-513	25
α-helix	517-545	29

Chain B: 0 helices, 2 β-strands

Element	Residues	Length	Sheet
β-strand	7-11	5	1
β-strand	19-23	5	1

Chain H: 5 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	8
β-strand	11-12	2	9
β-strand	18-25	8	8
β-strand	33-39	7	10
β-strand	45-52	8	10
β-strand	57-59	3	10
β-strand	66-72	7	8
β-strand	77-83	7	8
α-helix	87-89	3
β-strand	91-98	8	10
β-strand	105-108	4	10
β-strand	112-114	3	10
β-strand	115-116	2	9
β-strand	122	1	11
α-helix	123-124	2
β-strand	125-129	5	12
β-strand	140-150	11	12
β-strand	151	1	11
β-strand	156-159	4	13
α-helix	160-162	3
β-strand	168-170	3	12
α-helix	171-173	3
β-strand	174-176	3	12
β-strand	179-189	11	12
β-strand	199-204	6	13
α-helix	205-207	3
β-strand	209-214	6	13

Chain L: 8 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	2
β-strand	10-13	4	3
β-strand	19-25	7	2
β-strand	30-31	2	4
β-strand	34-35	2	4
β-strand	37-42	6	3
β-strand	49-53	5	3
β-strand	57-58	2	3
α-helix	59	1
β-strand	66-71	6	2
β-strand	74-79	6	2
α-helix	84-86	3
β-strand	88-94	7	3
α-helix	100	1
β-strand	101-102	2	3
β-strand	106-110	5	3
β-strand	115	1	5
α-helix	116-117	2
β-strand	118-122	5	6
α-helix	123-125	3
α-helix	126-130	5
β-strand	133-143	11	6
β-strand	144	1	5
β-strand	148-154	7	7
β-strand	157-159	3	7
β-strand	163-167	5	6
α-helix	168-171	4
β-strand	177-186	10	6
α-helix	187-190	4
β-strand	195-202	8	7
β-strand	209-214	6	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Hepcidin	B	protein	25	Homo sapiens	P81172 (AlphaFold model)
Solute carrier family 40 member 1	A	protein	605	Homo sapiens	Q9NP59 (AlphaFold model)
Fab45D8 Light Chain	L	protein	218	Mus musculus
Fab45D8 Heavy Chain	H	protein	220	Mus musculus

Sequence of entity 1 (B), FASTA

>6WBV_1 Hepcidin (chains B)
DTHFPICIFCCGCCHRSKCGMCCKT

Sequence of entity 2 (A), FASTA

>6WBV_2 Solute carrier family 40 member 1 (chains A)
MTRAGDHNRQRGCCGSLADYLTSAKFLLYLGHSLSTWGDRMWHFAVSVFLVELYGNSLLL
TAVYGLVVAGSVLVLGAIIGDWVDKNARLKVAQTSLVVQNVSVILCGIILMMVFLHKHEL
LTMYHGWVLTSCYILIITIANIANLASTATAITIQRDWIVVVAGEDRSKLANMNATIRRI
DQLTNILAPMAVGQIMTFGSPVIGCGFISGWNLVSMCVEYVLLWKVYQKTPALAVKAGLK
EEETELKQLNLHKDTEPKPLEGTHLMGVKDSNIHELEHEQEPTCASQMAEPFRTFRDGWV
SYYNQPVFLAGMGLAFLYMTVLGFDCITTGYAYTQGLSGSILSILMGASAITGIMGTVAF
TWLRRKCGLVRTGLISGLAQLSCLILCVISVFMPGSPLDLSVSPFEDIRSRFIQGESITP
TKIPEITTEIYMSNGSNSANIVPETSPESVPIISVSLLFAGVIAARIGLWSFDLTVTQLL
QENVIESERGIINGVQNSMNYLLDLLHFIMVILAPNPEAFGLLVLISVSFVAMGHIMYFR
FAQNTLGNKLFACGPDAKEVRKENQANTSVVGSGLEVLFQGPGAAEDQVDPRLIDGKHHH
HHHHH

Sequence of entity 3 (L), FASTA

>6WBV_3 Fab45D8 Light Chain (chains L)
DIVLTQSPASLPVSLGQRATISCRASKSVSASAYSYMHWYQQKPGQPPKPLIYLASNLES
GVPARFSGSGSGTDFTLNIHPVEEEDAATYYCQHNRELPYTFGGGTKLEIKRADAAPTVS
IFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMS
STLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC

Sequence of entity 4 (H), FASTA

>6WBV_4 Fab45D8 Heavy Chain (chains H)
EVQLQESGPGLAKPSQTLSLTCSVTGSSITSDYWNWIRKFPGNKLEYMGYISYSGSTYYN
PSLKSQISITRDTSKNHYYLQLNSVTTEDTATYYCARQGLRNWYFDVWGTGTTVTVSSAK
TTAPSVYPLAPVCGGTTGSSVTLGCLVKGYFPEPVTLTWNSGSLSSGVHTFPALLQSGLY
TLSSSVTVTSNTWPSQTITCNVAHPASSTKVDKKIEPRVP

Ligands and cofactors

ID	Name	Formula	Copies
CO	Cobalt (II) ion	Co	2
AGA	(1S)-2-{[{[(2S)-2,3-dihydroxypropyl]oxy}(hydroxy)phosphoryl]oxy}-1-[(pentanoylo…	C19 H36 O10 P	2

Primary citation

Structure of hepcidin-bound ferroportin reveals iron homeostatic mechanisms. Billesbolle, C.B., Azumaya, C.M., Kretsch, R.C. et al. Nature (2020) 586:807-811. DOI 10.1038/s41586-020-2668-z · PubMed

Other PDB entries of the same protein (UniProt P81172 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3H0T 1.89 Å, Hepcidin-Fab complex
4QAE 2.1 Å, Crystal structure of an engineered lipocalin (Anticalin) in complex with human hepcidin
1M4E Solution Structure of Hepcidin-20
1M4F Solution Structure of Hepcidin-25
2KEF Solution NMR structures of human hepcidin at 325K

Browse structure collections

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