6AYZ: Asf1-Fab 12E complex
Crystal structure of Asf1-Fab 12E complex. Determined by X-ray diffraction at 2.1 Å resolution. Released 17 Jan 2018.
- Method
- X-ray diffraction
- Resolution
- 2.1 Å
- Organisms
- Homo sapiens, Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
- Chains
- 6
- Atoms
- 9,637
- Mol. weight
- 128.99 kDa
- Released
- 17 Jan 2018
Explore 6AYZ in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
6AYZ contains 47 α-helices and 110 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: 6 helices, 10 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 5-11 | 7 | 24 |
| β-strand | 16-17 | 2 | 6 |
| α-helix | 21 | 1 | |
| β-strand | 22-29 | 8 | 24 |
| β-strand | 38-48 | 11 | 6 |
| β-strand | 51-62 | 12 | 6 |
| β-strand | 69-76 | 8 | 24 |
| α-helix | 77-79 | 3 | |
| α-helix | 81-83 | 3 | |
| α-helix | 86-89 | 4 | |
| β-strand | 92-101 | 10 | 6 |
| β-strand | 104-117 | 14 | 6 |
| α-helix | 120-124 | 5 | |
| α-helix | 132-134 | 3 | |
| β-strand | 135-139 | 5 | 6 |
| β-strand | 145-148 | 4 | 6 |
Chain B: 8 helices, 22 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-7 | 5 | 1 |
| β-strand | 10-12 | 3 | 2 |
| β-strand | 18-25 | 8 | 1 |
| β-strand | 34-39 | 6 | 2 |
| β-strand | 45-51 | 7 | 2 |
| β-strand | 58-60 | 3 | 2 |
| α-helix | 62-64 | 3 | |
| β-strand | 68-73 | 6 | 1 |
| β-strand | 78-83 | 6 | 1 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-100 | 9 | 2 |
| β-strand | 103-107 | 5 | 2 |
| β-strand | 111-115 | 5 | 2 |
| α-helix | 118-120 | 3 | |
| β-strand | 121 | 1 | 3 |
| α-helix | 122-123 | 2 | |
| β-strand | 124-128 | 5 | 4 |
| β-strand | 135-136 | 2 | 4 |
| β-strand | 139-149 | 11 | 4 |
| β-strand | 150 | 1 | 3 |
| β-strand | 155-158 | 4 | 5 |
| α-helix | 159-161 | 3 | |
| β-strand | 167-169 | 3 | 4 |
| α-helix | 170-172 | 3 | |
| β-strand | 173-174 | 2 | 4 |
| β-strand | 180-189 | 10 | 4 |
| α-helix | 190-192 | 3 | |
| β-strand | 199-204 | 6 | 5 |
| α-helix | 205-207 | 3 | |
| β-strand | 209-214 | 6 | 5 |
Chain C: 9 helices, 21 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-7 | 4 | 6 |
| β-strand | 10-13 | 4 | 7 |
| β-strand | 18-25 | 8 | 6 |
| α-helix | 30-32 | 3 | |
| β-strand | 33-38 | 6 | 7 |
| β-strand | 45-49 | 5 | 7 |
| β-strand | 53-54 | 2 | 7 |
| α-helix | 55 | 1 | |
| β-strand | 62-67 | 6 | 6 |
| β-strand | 70-75 | 6 | 6 |
| α-helix | 80-82 | 3 | |
| β-strand | 85-91 | 7 | 7 |
| β-strand | 96-98 | 3 | 7 |
| β-strand | 102-106 | 5 | 7 |
| α-helix | 107 | 1 | |
| β-strand | 111 | 1 | 8 |
| α-helix | 112-113 | 2 | |
| β-strand | 114-118 | 5 | 9 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-126 | 5 | |
| β-strand | 129-139 | 11 | 9 |
| β-strand | 140 | 1 | 8 |
| β-strand | 145-150 | 6 | 10 |
| β-strand | 153-154 | 2 | 10 |
| β-strand | 159-163 | 5 | 9 |
| α-helix | 164-167 | 4 | |
| β-strand | 173-182 | 10 | 9 |
| α-helix | 183-186 | 4 | |
| β-strand | 191-197 | 7 | 10 |
| β-strand | 205-210 | 6 | 10 |
Chain D: 9 helices, 21 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 5-7 | 3 | 11 |
| β-strand | 10-13 | 4 | 12 |
| β-strand | 18-24 | 7 | 11 |
| α-helix | 30-32 | 3 | |
| β-strand | 33-38 | 6 | 12 |
| β-strand | 45-49 | 5 | 12 |
| β-strand | 53-54 | 2 | 12 |
| α-helix | 55 | 1 | |
| β-strand | 62-67 | 6 | 11 |
| β-strand | 70-75 | 6 | 11 |
| α-helix | 80-82 | 3 | |
| β-strand | 85-91 | 7 | 12 |
| β-strand | 96-98 | 3 | 12 |
| β-strand | 102-106 | 5 | 12 |
| β-strand | 111 | 1 | 13 |
| α-helix | 112-113 | 2 | |
| β-strand | 114-118 | 5 | 14 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-127 | 6 | |
| β-strand | 129-139 | 11 | 14 |
| β-strand | 140 | 1 | 13 |
| β-strand | 145-150 | 6 | 15 |
| β-strand | 153-154 | 2 | 15 |
| α-helix | 155 | 1 | |
| β-strand | 159-163 | 5 | 14 |
| α-helix | 164-167 | 4 | |
| β-strand | 173-182 | 10 | 14 |
| α-helix | 183-187 | 5 | |
| β-strand | 191-197 | 7 | 15 |
| β-strand | 205-210 | 6 | 15 |
Chain M: 7 helices, 12 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-11 | 8 | 16 |
| β-strand | 16-17 | 2 | 11 |
| α-helix | 21 | 1 | |
| β-strand | 22-30 | 9 | 16 |
| β-strand | 34 | 1 | 17 |
| β-strand | 38-48 | 11 | 11 |
| β-strand | 51-62 | 12 | 11 |
| β-strand | 65 | 1 | 17 |
| α-helix | 66 | 1 | |
| β-strand | 68-76 | 9 | 16 |
| α-helix | 77-79 | 3 | |
| α-helix | 81-83 | 3 | |
| α-helix | 86-90 | 5 | |
| β-strand | 93-101 | 9 | 11 |
| β-strand | 104-117 | 14 | 11 |
| α-helix | 120-124 | 5 | |
| α-helix | 132-134 | 3 | |
| β-strand | 135-139 | 5 | 11 |
| β-strand | 145-148 | 4 | 11 |
Chain R: 8 helices, 24 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-7 | 5 | 18 |
| β-strand | 11-12 | 2 | 19 |
| β-strand | 18-25 | 8 | 18 |
| β-strand | 34-39 | 6 | 20 |
| β-strand | 45-51 | 7 | 20 |
| β-strand | 58-60 | 3 | 20 |
| β-strand | 68-73 | 6 | 18 |
| β-strand | 78-83 | 6 | 18 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-100 | 9 | 20 |
| β-strand | 103-107 | 5 | 20 |
| β-strand | 111-113 | 3 | 20 |
| β-strand | 114-115 | 2 | 19 |
| α-helix | 118-120 | 3 | |
| β-strand | 121 | 1 | 21 |
| α-helix | 122-123 | 2 | |
| β-strand | 124-128 | 5 | 22 |
| β-strand | 135-136 | 2 | 22 |
| β-strand | 139-149 | 11 | 22 |
| β-strand | 150 | 1 | 21 |
| β-strand | 155-158 | 4 | 23 |
| α-helix | 159-161 | 3 | |
| β-strand | 163 | 1 | 23 |
| β-strand | 167-169 | 3 | 22 |
| α-helix | 170-172 | 3 | |
| β-strand | 173-174 | 2 | 22 |
| β-strand | 180-189 | 10 | 22 |
| α-helix | 190-192 | 3 | |
| β-strand | 199-204 | 6 | 23 |
| α-helix | 205-207 | 3 | |
| β-strand | 209-214 | 6 | 23 |
| α-helix | 217-219 | 3 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Fab Heavy Chain | B, R | protein | 224 | Homo sapiens | |
| Fab Light Chain | C, D | protein | 215 | Homo sapiens | |
| Histone chaperone ASF1 | A, M | protein | 154 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P32447 (AlphaFold model) |
Sequence of entity 1 (B, R), FASTA
>6AYZ_1 Fab Heavy Chain (chains B, R)
EISEVQLVESGGGLVQPGGSLRLSCAASGFNVSYYSIHWVRQAPGKGLEWVASIYPYYGS
TSYADSVKGRFTISADTSKNTAYLQMNSLRAEDTAVYYCARGYGWALDYWGQGTLVTVSS
ASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSS
GLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCD
Sequence of entity 2 (C, D), FASTA
>6AYZ_2 Fab Light Chain (chains C, D)
SDIQMTQSPSSLSASVGDRVTITCRASQSVSSAVAWYQQKPGKAPKLLIYSASSLYSGVP
SRFSGSRSGTDFTLTISSLQPEDFATYYCQQDGWSLITFGQGTKVEIKRTVAAPSVFIFP
PSDSQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTL
TLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
Sequence of entity 3 (A, M), FASTA
>6AYZ_3 Histone chaperone ASF1 (chains A, M)
GSIVSLLGIKVLNNPAKFTDPYEFEITFECLESLKHDLEWKLTYVGSSRSLDHDQELDSI
LVGPVPVGVNKFVFSADPPSAELIPASELVSVTVILLSCSYDGREFVRVGYYVNNEYDEE
ELRENPPAKVQVDHIVRNILAEKPRVTRFNIVWD
Primary citation
Locking the Elbow: Improved Antibody Fab Fragments as Chaperones for Structure Determination. Bailey, L.J., Sheehy, K.M., Dominik, P.K. et al. J Mol Biol (2018) 430:337-347. DOI 10.1016/j.jmb.2017.12.012 · PubMed
Other PDB entries of the same protein (UniProt P32447 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 1ROC 1.5 Å, Crystal structure of the histone deposition protein Asf1
- 5UCB 1.52 Å, Structure of antigen-Fab complex with engineered switch residue region.
- 2HUE 1.7 Å, Structure of the H3-H4 chaperone Asf1 bound to histones H3 and H4
- 5UEK 1.7 Å, Structure of antigen-Fab 12E complex with Histone chaperone ASF1
- 5UEA 1.7 Å, Structure of antigen-Fab complex with Histone chaperone ASF1
- 2IDC 2.2 Å, Structure of the Histone H3-Asf1 Chaperone Interaction
- 4ZBJ 2.25 Å, UBN1 peptide bound to H3.3/H4/Asf1
- 4EO5 2.35 Å, Yeast Asf1 bound to H3/H4G94P mutant
- 5EII 2.44 Å, Structural determination of an protein complex of a Fab with increased solubility
- 6AZ2 2.48 Å, Crystal structure of Asf1-Fab 12E complex
- 4RRP 2.79 Å, Crystal Structure of the Fab complexed with antigen Asf1p, Northeast Structural Genomics…
- 9AWE 2.8 Å, The crystal structure of an engineered Protein GF with Human Kappa Fab
Browse structure collections
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