1AV1: Human apolipoprotein a-I

Crystal structure of human apolipoprotein a-I. Determined by X-ray diffraction at 4.0 Å resolution. Released 4 Feb 1998.

Method
X-ray diffraction
Resolution
4.0 Å
Organism
Homo sapiens
Chains
4
Atoms
6,588
Mol. weight
93.76 kDa
Released
4 Feb 1998

Explore 1AV1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1AV1 contains 40 α-helices and 0 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.

Chains A and C: 10 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix49-535
α-helix54-585
α-helix59-624
α-helix66-705
α-helix72-14069
α-helix143-1442
α-helix145-1495
α-helix150-21061
α-helix213-2175
α-helix229-24214
Chains B and D: 10 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix45-484
α-helix49-546
α-helix57-637
α-helix661
α-helix67-726
α-helix73-11745
α-helix120-14122
α-helix144-20158
α-helix208-21811
α-helix228-23912

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Apolipoprotein a-IA, B, C, Dprotein201Homo sapiensP02647 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>1AV1_1 APOLIPOPROTEIN A-I (chains A, B, C, D)
MLKLLDNWDSVTSTFSKLREQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLD
DFQKKWQEEMELYRQKVEPLRAELQEGARQKLHELQEKLSPLGEEMRDRARAHVDALRTH
LAPYSDELRQRLAARLEALKENGGARLAEYHAKATEHLSTLSEKAKPALEDLRQGLLPVL
ESFKVSFLSALEEYTKKLNTQ

Primary citation

Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation. Borhani, D.W., Rogers, D.P., Engler, J.A. et al. Proc Natl Acad Sci U S A (1997) 94:12291-12296. DOI 10.1073/pnas.94.23.12291 · PubMed

Other PDB entries of the same protein (UniProt P02647 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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