6FGB: Human FcRn extra-cellular domain

Human FcRn extra-cellular domain complexed with Fab fragment of Rozanolixizumab. Determined by X-ray diffraction at 2.9 Å resolution. Released 29 Aug 2018.

Method
X-ray diffraction
Resolution
2.9 Å
Organism
Homo sapiens
Chains
4
Atoms
6,141
Mol. weight
97.35 kDa
Released
29 Aug 2018

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

Secondary structure: helices and β-sheets

6FGB contains 25 α-helices and 74 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: 9 helices, 18 β-strands

ElementResiduesLengthSheet
β-strand6-1491
α-helix17-182
β-strand24-3071
β-strand33-3971
β-strand46-4721
α-helix49-535
α-helix60-8122
β-strand89-98101
β-strand104-11291
β-strand115-12171
β-strand126-12831
α-helix132-14211
α-helix147-1537
α-helix154-1585
α-helix159-16911
α-helix171-1755
β-strand17812
α-helix179-1802
β-strand181-18883
β-strand193-203113
β-strand20412
β-strand208-21474
β-strand217-21824
β-strand223-22863
β-strand234-243103
β-strand250-25674
β-strand263-26644
Chain B: 1 helix, 11 β-strands
ElementResiduesLengthSheet
β-strand315
α-helix4-52
β-strand6-1166
β-strand21-30106
β-strand3115
β-strand36-4167
β-strand44-4527
β-strand50-5126
β-strand55-5626
β-strand62-7096
β-strand78-8367
β-strand91-9447
Chain H: 9 helices, 21 β-strands
ElementResiduesLengthSheet
β-strand6-7215
β-strand10-12316
β-strand18-23615
α-helix29-313
β-strand34-39616
β-strand46-51616
β-strand58-60316
β-strand68-73615
α-helix74-763
β-strand78-83615
α-helix88-903
β-strand92-98716
β-strand111-115516
α-helix119-1202
β-strand121117
α-helix122-1232
β-strand124-128518
α-helix129-1313
β-strand139-1491118
β-strand150117
β-strand155-158419
α-helix159-1613
β-strand167-169318
α-helix170-1723
β-strand173-175318
β-strand179-1891118
α-helix192-1954
β-strand196120
β-strand199-204619
β-strand209-214619
Chain L: 6 helices, 24 β-strands
ElementResiduesLengthSheet
β-strand4-748
β-strand10-1459
β-strand19-2578
β-strand30110
β-strand36110
β-strand38-4369
β-strand50-5459
β-strand58-5929
α-helix601
β-strand67-7158
β-strand75-8068
α-helix85-873
β-strand89-9579
β-strand102-10329
β-strand107-11269
β-strand116111
β-strand119-123512
α-helix124-1263
α-helix127-1315
β-strand134-1441112
β-strand145111
β-strand149-153513
β-strand154-155214
β-strand158-159214
β-strand164-168512
α-helix169-1724
β-strand178-1871012
α-helix188-1936
β-strand196-203813
β-strand210-215613

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
IgG receptor FcRn large subunit p51Aprotein342Homo sapiensP55899 (AlphaFold model)
Beta-2-microglobulinBprotein99Homo sapiensP61769 (AlphaFold model)
1519.g57- Light chainLprotein219Homo sapiens
1519.g57- Heavy chainHprotein228Homo sapiens
Sequence of entity 1 (A), FASTA
>6FGB_1 IgG receptor FcRn large subunit p51 (chains A)
AESHLSLLYHLTAVSSPAPGTPAFWVSGWLGPQQYLSYNSLRGEAEPCGAWVWENQVSWY
WEKETTDLRIKEKLFLEAFKALGGKGPYTLQGLLGCELGPDNTSVPTAKFALNGEEFMNF
DLKQGTWGGDWPEALAISQRWQQQDKAANKELTFLLFSCPHRLREHLERGRGNLEWKEPP
SMRLKARPSSPGFSVLTCSAFSFYPPELQLRFLRNGLAAGTGQGDFGPNSDGSFHASSSL
TVKSGDEHHYCCIVQHAGLAQPLRVELESPAKSSVLVVGIVIGVLLLTAAAVGGALLWRR
MRSGLPAPWISLRGDDTGVLLPTPGEAQDADLKDVNVIPATA
Sequence of entity 2 (B), FASTA
>6FGB_2 Beta-2-microglobulin (chains B)
IQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDW
SFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM
Sequence of entity 3 (L), FASTA
>6FGB_3 1519.g57- Light chain (chains L)
DIQMTQSPSSLSASVGDRVTITCKSSQSLVGASGKTYLYWLFQKPGKAPKRLIYLVSTLD
SGIPSRFSGSGSGTEFTLTISSLQPEDFATYYCLQGTHFPHTFGQGTKLEIKRTVAAPSV
FIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSL
SSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
Sequence of entity 4 (H), FASTA
>6FGB_4 1519.g57- Heavy chain (chains H)
EVPLVESGGGLVQPGGSLRLSCAVSGFTFSNYGMVWVRQAPGKGLEWVAYIDSDGDNTYY
RDSVKGRFTISRDNAKSSLYLQMNSLRAEDTAVYYCTTGIVRPFLYWGQGTLVTVSSAST
KGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLY
SLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCAA

Primary citation

Generation and characterization of a high affinity anti-human FcRn antibody, rozanolixizumab, and the effects of different molecular formats on the reduction of plasma IgG concentration. Smith, B., Kiessling, A., Lledo-Garcia, R. et al. MAbs (2018) 10:1111-1130. DOI 10.1080/19420862.2018.1505464 · PubMed

Other PDB entries of the same protein (UniProt P55899 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

About this viewer

MolViewer shows 6FGB directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.