5EII: Fab Heavy Chain
Structural determination of an protein complex of a Fab with increased solubility. Determined by X-ray diffraction at 2.44 Å resolution. Released 9 Nov 2016.
- Method
- X-ray diffraction
- Resolution
- 2.44 Å
- Organisms
- Homo sapiens, Saccharomyces cerevisiae
- Chains
- 6
- Atoms
- 9,056
- Mol. weight
- 132.26 kDa
- Released
- 9 Nov 2016
Explore 5EII in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
5EII contains 45 α-helices and 113 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: 10 helices, 25 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-7 | 5 | 1 |
| β-strand | 10-12 | 3 | 2 |
| β-strand | 18-25 | 8 | 1 |
| α-helix | 29-31 | 3 | |
| β-strand | 32-39 | 8 | 2 |
| β-strand | 46-52 | 7 | 2 |
| β-strand | 57-60 | 4 | 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 | 92-101 | 10 | 2 |
| β-strand | 102-103 | 2 | 3 |
| β-strand | 111-114 | 4 | 2 |
| β-strand | 118-122 | 5 | 2 |
| α-helix | 125-127 | 3 | |
| β-strand | 128 | 1 | 4 |
| α-helix | 129-130 | 2 | |
| β-strand | 131-135 | 5 | 5 |
| α-helix | 136-138 | 3 | |
| β-strand | 147-156 | 10 | 5 |
| β-strand | 157 | 1 | 4 |
| β-strand | 162-165 | 4 | 6 |
| α-helix | 166-168 | 3 | |
| β-strand | 170 | 1 | 6 |
| β-strand | 174-176 | 3 | 5 |
| α-helix | 177-179 | 3 | |
| β-strand | 180-181 | 2 | 5 |
| β-strand | 187-195 | 9 | 5 |
| α-helix | 197-199 | 3 | |
| β-strand | 200 | 1 | 7 |
| β-strand | 203 | 1 | 7 |
| β-strand | 206-211 | 6 | 6 |
| α-helix | 212-214 | 3 | |
| β-strand | 216-221 | 6 | 6 |
Chain B: 8 helices, 21 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-7 | 4 | 8 |
| β-strand | 10-13 | 4 | 9 |
| β-strand | 19-25 | 7 | 8 |
| β-strand | 33-38 | 6 | 9 |
| β-strand | 45-49 | 5 | 9 |
| β-strand | 53-54 | 2 | 9 |
| α-helix | 55 | 1 | |
| β-strand | 62-67 | 6 | 8 |
| β-strand | 70-75 | 6 | 8 |
| α-helix | 80-82 | 3 | |
| β-strand | 85-90 | 6 | 9 |
| α-helix | 96 | 1 | |
| β-strand | 97-98 | 2 | 9 |
| β-strand | 102-106 | 5 | 9 |
| β-strand | 111 | 1 | 10 |
| α-helix | 112-113 | 2 | |
| β-strand | 114-118 | 5 | 11 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-125 | 4 | |
| β-strand | 129-139 | 11 | 11 |
| β-strand | 140 | 1 | 10 |
| β-strand | 144-150 | 7 | 12 |
| β-strand | 153-154 | 2 | 12 |
| β-strand | 159-163 | 5 | 11 |
| α-helix | 164-167 | 4 | |
| β-strand | 173-182 | 10 | 11 |
| α-helix | 183-187 | 5 | |
| β-strand | 191-198 | 8 | 12 |
| β-strand | 205-210 | 6 | 12 |
Chain G: 5 helices, 10 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-11 | 8 | 13 |
| β-strand | 16-17 | 2 | 14 |
| β-strand | 22-30 | 9 | 13 |
| β-strand | 38-44 | 7 | 14 |
| β-strand | 55-62 | 8 | 14 |
| α-helix | 65-66 | 2 | |
| β-strand | 68-76 | 9 | 13 |
| α-helix | 77-80 | 4 | |
| α-helix | 81-83 | 3 | |
| β-strand | 92-101 | 10 | 14 |
| β-strand | 104-117 | 14 | 14 |
| α-helix | 120-124 | 5 | |
| α-helix | 132-134 | 3 | |
| β-strand | 135-139 | 5 | 14 |
| β-strand | 145-148 | 4 | 14 |
Chain H: 11 helices, 24 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-7 | 5 | 15 |
| β-strand | 10-12 | 3 | 16 |
| β-strand | 18-25 | 8 | 15 |
| β-strand | 32-39 | 8 | 16 |
| β-strand | 46-52 | 7 | 16 |
| α-helix | 53-55 | 3 | |
| β-strand | 57-60 | 4 | 16 |
| α-helix | 62-64 | 3 | |
| β-strand | 65 | 1 | 15 |
| β-strand | 68-73 | 6 | 15 |
| β-strand | 78-83 | 6 | 15 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-101 | 10 | 16 |
| β-strand | 102-103 | 2 | 13 |
| β-strand | 111-114 | 4 | 16 |
| β-strand | 118-122 | 5 | 16 |
| α-helix | 125-127 | 3 | |
| β-strand | 128 | 1 | 17 |
| α-helix | 129-130 | 2 | |
| β-strand | 131-135 | 5 | 18 |
| α-helix | 136-138 | 3 | |
| α-helix | 141-142 | 2 | |
| β-strand | 146-156 | 11 | 18 |
| β-strand | 157 | 1 | 17 |
| β-strand | 162-165 | 4 | 19 |
| α-helix | 166-168 | 3 | |
| β-strand | 170 | 1 | 19 |
| β-strand | 174-176 | 3 | 18 |
| α-helix | 177-179 | 3 | |
| β-strand | 180-181 | 2 | 18 |
| β-strand | 187-196 | 10 | 18 |
| α-helix | 197-199 | 3 | |
| β-strand | 206-211 | 6 | 19 |
| α-helix | 212-214 | 3 | |
| β-strand | 216-221 | 6 | 19 |
Chain I: 3 helices, 12 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-11 | 8 | 3 |
| β-strand | 16-17 | 2 | 20 |
| α-helix | 21 | 1 | |
| β-strand | 22-30 | 9 | 3 |
| β-strand | 38-44 | 7 | 21 |
| β-strand | 55-62 | 8 | 21 |
| α-helix | 65-66 | 2 | |
| β-strand | 68-76 | 9 | 3 |
| α-helix | 77-80 | 4 | |
| β-strand | 98-101 | 4 | 21 |
| β-strand | 104-110 | 7 | 21 |
| β-strand | 113 | 1 | 22 |
| β-strand | 136-137 | 2 | 20 |
| β-strand | 139 | 1 | 22 |
| β-strand | 145-148 | 4 | 21 |
Chain L: 8 helices, 21 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-7 | 4 | 23 |
| β-strand | 10-13 | 4 | 24 |
| β-strand | 19-25 | 7 | 23 |
| β-strand | 33-38 | 6 | 24 |
| β-strand | 45-49 | 5 | 24 |
| β-strand | 53-54 | 2 | 24 |
| α-helix | 55 | 1 | |
| β-strand | 62-67 | 6 | 23 |
| β-strand | 70-75 | 6 | 23 |
| α-helix | 80-82 | 3 | |
| β-strand | 85-90 | 6 | 24 |
| α-helix | 96 | 1 | |
| β-strand | 97-98 | 2 | 24 |
| β-strand | 102-106 | 5 | 24 |
| β-strand | 111 | 1 | 25 |
| α-helix | 112-113 | 2 | |
| β-strand | 114-118 | 5 | 26 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-125 | 4 | |
| β-strand | 129-139 | 11 | 26 |
| β-strand | 140 | 1 | 25 |
| β-strand | 145-150 | 6 | 27 |
| β-strand | 153-155 | 3 | 27 |
| β-strand | 159-163 | 5 | 26 |
| α-helix | 164-167 | 4 | |
| β-strand | 173-182 | 10 | 26 |
| α-helix | 183-186 | 4 | |
| β-strand | 191-197 | 7 | 27 |
| β-strand | 205-210 | 6 | 27 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Fab Heavy Chain | A, H | protein | 235 | Homo sapiens | |
| Fab Light Chain | B, L | protein | 215 | Homo sapiens | |
| Histone chaperone ASF1 | G, I | protein | 156 | Saccharomyces cerevisiae | P32447 (AlphaFold model) |
Sequence of entity 1 (A, H), FASTA
>5EII_1 Fab Heavy Chain (chains A, H)
EISEVQLVESGGGLVQPGGSLRLSCAASGFNISYSSIHWVRQAPGKGLEWVASISSYYGS
TYYADSVKGRFTISADTSKNTAYLQMNSLRAEDTAVYYCARSRGQASWDYWWAMDYWGQG
TLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTF
PAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHT
Sequence of entity 2 (B, L), FASTA
>5EII_2 Fab Light Chain (chains B, L)
SDIQMTQSPSSLSASVGDRVTITCRASQSVSSAVAWYQQKPGKAPKLLIYSASSLYSGVP
SRFSGSRSGTDFTLTISSLQPEDFATYYCQQSSDDPITFGQGTKVEIKRTVAAPSVFIFP
PSDSQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTL
TLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
Sequence of entity 3 (G, I), FASTA
>5EII_3 Histone chaperone ASF1 (chains G, I)
MSIVSLLGIKVLNNPAKFTDPYEFEITFECLESLKHDLEWKLTYVGSSRSLDHDQELDSI
LVGPVPVGVNKFVFSADPPSAELIPASELVSVTVILLSCSYDGREFVRVGYYVNNEYDEE
ELRENPPAKVQVDHIVRNILAEKPRVTRFNIVWDNE
Primary citation
Structural determination of an protein complex of a Fab with increased solubility. Bailey, L.J., Kossiakoff, A.A., Schaefer, Z.P. To be published.
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
- 6AYZ 2.1 Å, Crystal structure of Asf1-Fab 12E complex
- 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
- 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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