4K71: High affinity Human Serum Albumin variant

Crystal structure of a high affinity Human Serum Albumin variant bound to the Neonatal Fc Receptor. Determined by X-ray diffraction at 2.4 Å resolution. Released 23 Oct 2013.

Method
X-ray diffraction
Resolution
2.4 Å
Organism
Homo sapiens
Chains
6
Atoms
15,259
Mol. weight
219.08 kDa
Released
23 Oct 2013

Explore 4K71 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4K71 contains 99 α-helices and 60 β-strands across 6 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: 38 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix6-149
α-helix16-3015
α-helix36-5520
α-helix66-749
α-helix81-844
α-helix87-915
α-helix97-1048
α-helix120-12910
α-helix131-14515
α-helix151-16818
α-helix174-20633
α-helix208-22215
α-helix228-24619
α-helix250-26617
α-helix268-2703
α-helix278-2803
α-helix283-29210
α-helix293-2997
α-helix302-3043
α-helix305-3062
α-helix307-3115
α-helix315-3217
α-helix323-33715
α-helix343-36018
α-helix366-3705
α-helix373-3764
α-helix377-41438
α-helix420-43718
α-helix442-46625
α-helix471-4788
α-helix484-4907
α-helix498-5025
α-helix504-5063
α-helix511-5133
α-helix518-53518
α-helix541-56020
α-helix564-5707
α-helix572-58211
Chain B: 10 helices, 19 β-strands
ElementResiduesLengthSheet
β-strand6-1491
α-helix17-182
β-strand24-3071
β-strand33-3971
β-strand46-4721
α-helix49-535
α-helix60-8223
β-strand89-98101
β-strand104-11291
β-strand115-12171
β-strand126-12831
α-helix132-14312
α-helix147-1537
α-helix154-1585
α-helix159-16911
α-helix171-1744
β-strand17812
α-helix179-1802
β-strand181-190103
β-strand193-203113
β-strand20412
β-strand208-21474
β-strand217-22044
β-strand223-22863
β-strand234-243103
α-helix247-2493
β-strand250-25674
β-strand263-26534
β-strand26713
Chain C: 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 D: 38 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix6-149
α-helix16-3015
α-helix36-5520
α-helix66-749
α-helix81-844
α-helix87-915
α-helix941
α-helix97-1048
α-helix120-12910
α-helix131-14515
α-helix151-16818
α-helix174-20128
α-helix202-2065
α-helix208-22215
α-helix228-24619
α-helix250-26617
α-helix268-2714
α-helix278-2803
α-helix283-29210
α-helix293-2997
α-helix3061
α-helix307-3115
α-helix315-3217
α-helix323-33715
α-helix343-36119
α-helix366-3694
α-helix374-3763
α-helix377-41438
α-helix420-43819
α-helix442-46625
α-helix471-4788
α-helix484-4907
α-helix499-5024
α-helix511-5133
α-helix518-53518
α-helix541-55818
α-helix567-5704
α-helix572-58211
Chain E: 10 helices, 19 β-strands
ElementResiduesLengthSheet
β-strand6-1498
α-helix17-182
β-strand24-3078
β-strand33-3978
β-strand46-4728
α-helix49-535
α-helix60-8223
β-strand89-98108
β-strand104-11298
β-strand115-12178
β-strand126-12838
α-helix132-14312
α-helix147-1537
α-helix154-1585
α-helix159-16911
α-helix171-1744
β-strand17819
α-helix179-1802
β-strand181-1901010
β-strand193-2031110
β-strand20419
β-strand209-214611
β-strand217-220411
β-strand223-228610
β-strand234-2431010
α-helix247-2493
β-strand250-255611
β-strand263-265311
β-strand267110
Chain F: 2 helices, 11 β-strands
ElementResiduesLengthSheet
β-strand3112
α-helix4-52
β-strand6-11613
β-strand21-301013
β-strand31112
β-strand36-41614
β-strand44-45214
α-helix461
β-strand50-51213
β-strand55-56213
β-strand62-70913
β-strand78-83614
β-strand91-94414

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Serum albuminA, Dprotein585Homo sapiensP02768 (AlphaFold model)
IgG receptor FcRn large subunit p51B, Eprotein274Homo sapiensP55899 (AlphaFold model)
Beta-2-microglobulinC, Fprotein99Homo sapiensP61769 (AlphaFold model)
Sequence of entity 1 (A, D), FASTA
>4K71_1 Serum albumin (chains A, D)
DAHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKTCVADESAE
NCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEPERNECFLQHKDDNPNLPRLVRPEV
DVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAKRYKAAFTECCQAADKAACLLP
KLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAVARLSQRFPKAEFAEVSKLVTDLTK
VHTECCHGDLLECADDRADLAKYICENQDSISSKLKECCEKPLLEKSHCIAEVENDEMPA
DLPSLAADFVESKDVCKNYAEAKDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKC
CAAADPHECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEYKFQNALLVRYTKKVPQMSA
PTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVVLNQLCVLHEKTPVSDRVTKCCTES
LVNRRPCFSALEVDETYVPKEFNAGTFTFHADICTLSEKERQIKKQTALVELVKHKPKAT
KEQLKAAMDDFAAFVEKCCKADDKETCFAEEGKKLVAASQAALGL
Sequence of entity 2 (B, E), FASTA
>4K71_2 IgG receptor FcRn large subunit p51 (chains B, E)
AESHLSLLYHLTAVSSPAPGTPAFWVSGWLGPQQYLSYNSLRGEAEPCGAWVWENQVSWY
WEKETTDLRIKEKLFLEAFKALGGKGPYTLQGLLGCELGPDNTSVPTAKFALNGEEFMNF
DLKQGTWGGDWPEALAISQRWQQQDKAANKELTFLLFSCPHRLREHLERGRGNLEWKEPP
SMRLKARPSSPGFSVLTCSAFSFYPPELQLRFLRNGLAAGTGQGDFGPNSDGSFHASSSL
TVKSGDEHHYCCIVQHAGLAQPLRVELESPAKSS
Sequence of entity 3 (C, F), FASTA
>4K71_3 Beta-2-microglobulin (chains C, F)
IQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDW
SFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM

Primary citation

Crystal structure of an HSA/FcRn complex reveals recycling by competitive mimicry of HSA ligands at a pH-dependent hydrophobic interface. Schmidt, M.M., Townson, S.A., Andreucci, A.J. et al. Structure (2013) 21:1966-1978. DOI 10.1016/j.str.2013.08.022 · PubMed

Other PDB entries of the same protein (UniProt P02768 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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