6BFT: Bevacizumab Fab mutant
Structure of Bevacizumab Fab mutant in complex with VEGF. Determined by X-ray diffraction at 2.55 Å resolution. Released 31 Oct 2018.
- Method
- X-ray diffraction
- Resolution
- 2.55 Å
- Organism
- Homo sapiens
- Chains
- 6
- Atoms
- 8,359
- Mol. weight
- 121.34 kDa
- Released
- 31 Oct 2018
Explore 6BFT in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
6BFT contains 47 α-helices and 107 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: 12 helices, 25 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-7 | 5 | 6 |
| β-strand | 10-12 | 3 | 7 |
| β-strand | 18-25 | 8 | 6 |
| α-helix | 29-31 | 3 | |
| β-strand | 32 | 1 | 8 |
| β-strand | 34-39 | 6 | 7 |
| β-strand | 45-51 | 7 | 7 |
| β-strand | 58-60 | 3 | 7 |
| α-helix | 62-64 | 3 | |
| β-strand | 68-73 | 6 | 6 |
| α-helix | 74-76 | 3 | |
| β-strand | 78-83 | 6 | 6 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-98 | 7 | 7 |
| α-helix | 99-101 | 3 | |
| β-strand | 102 | 1 | 8 |
| β-strand | 112-113 | 2 | 7 |
| β-strand | 114 | 1 | 6 |
| β-strand | 117-121 | 5 | 7 |
| α-helix | 124-126 | 3 | |
| β-strand | 127 | 1 | 9 |
| α-helix | 128-129 | 2 | |
| β-strand | 130-134 | 5 | 10 |
| β-strand | 145-155 | 11 | 10 |
| β-strand | 156 | 1 | 9 |
| β-strand | 161-164 | 4 | 11 |
| α-helix | 165-167 | 3 | |
| β-strand | 169 | 1 | 11 |
| β-strand | 173-175 | 3 | 10 |
| α-helix | 176-178 | 3 | |
| β-strand | 179-180 | 2 | 10 |
| β-strand | 186-195 | 10 | 10 |
| α-helix | 196-198 | 3 | |
| β-strand | 205-210 | 6 | 11 |
| α-helix | 211-213 | 3 | |
| β-strand | 215-220 | 6 | 11 |
| α-helix | 223-225 | 3 | |
Chain B: 10 helices, 21 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-3 | 2 | |
| β-strand | 4-7 | 4 | 1 |
| β-strand | 10-14 | 5 | 2 |
| β-strand | 19-25 | 7 | 1 |
| β-strand | 33-38 | 6 | 2 |
| β-strand | 45-49 | 5 | 2 |
| β-strand | 53-54 | 2 | 2 |
| α-helix | 55 | 1 | |
| β-strand | 62-67 | 6 | 1 |
| β-strand | 70-75 | 6 | 1 |
| α-helix | 80-82 | 3 | |
| β-strand | 84-90 | 7 | 2 |
| α-helix | 96 | 1 | |
| β-strand | 97-98 | 2 | 2 |
| β-strand | 102-107 | 6 | 2 |
| β-strand | 111 | 1 | 3 |
| α-helix | 112-113 | 2 | |
| β-strand | 114-118 | 5 | 4 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-126 | 5 | |
| β-strand | 129-139 | 11 | 4 |
| β-strand | 140 | 1 | 3 |
| β-strand | 145-150 | 6 | 5 |
| β-strand | 153-154 | 2 | 5 |
| α-helix | 155 | 1 | |
| β-strand | 159-163 | 5 | 4 |
| α-helix | 164-167 | 4 | |
| β-strand | 173-182 | 10 | 4 |
| α-helix | 183-188 | 6 | |
| β-strand | 191-197 | 7 | 5 |
| β-strand | 205-210 | 6 | 5 |
Chain C: 3 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 15 | 1 | 8 |
| α-helix | 17-24 | 8 | |
| β-strand | 25 | 1 | 25 |
| β-strand | 27-34 | 8 | 26 |
| α-helix | 35-38 | 4 | |
| α-helix | 45 | 1 | |
| β-strand | 46-48 | 3 | 19 |
| β-strand | 51-58 | 8 | 26 |
| β-strand | 60 | 1 | 25 |
| β-strand | 66-84 | 19 | 19 |
| β-strand | 88-106 | 19 | 19 |
Chain G: 3 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 14-15 | 2 | 19 |
| α-helix | 16 | 1 | |
| α-helix | 17-24 | 8 | |
| β-strand | 25 | 1 | 23 |
| β-strand | 27-34 | 8 | 24 |
| α-helix | 35-38 | 4 | |
| β-strand | 46-48 | 3 | 8 |
| β-strand | 51-58 | 8 | 24 |
| β-strand | 60 | 1 | 23 |
| β-strand | 66-84 | 19 | 8 |
| β-strand | 88-106 | 19 | 8 |
Chain H: 10 helices, 24 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-7 | 5 | 17 |
| β-strand | 10-12 | 3 | 18 |
| β-strand | 18-25 | 8 | 17 |
| α-helix | 29-31 | 3 | |
| β-strand | 34-39 | 6 | 18 |
| β-strand | 46-51 | 6 | 18 |
| β-strand | 58-60 | 3 | 18 |
| α-helix | 62-64 | 3 | |
| β-strand | 68-73 | 6 | 17 |
| α-helix | 74-76 | 3 | |
| β-strand | 78-83 | 6 | 17 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-98 | 7 | 18 |
| α-helix | 99-101 | 3 | |
| β-strand | 102-103 | 2 | 19 |
| β-strand | 105 | 1 | 19 |
| β-strand | 112-113 | 2 | 18 |
| β-strand | 117-121 | 5 | 18 |
| α-helix | 125-126 | 2 | |
| β-strand | 127 | 1 | 20 |
| α-helix | 128-129 | 2 | |
| β-strand | 130-134 | 5 | 21 |
| β-strand | 145-155 | 11 | 21 |
| β-strand | 156 | 1 | 20 |
| β-strand | 161-164 | 4 | 22 |
| α-helix | 165-167 | 3 | |
| β-strand | 169 | 1 | 22 |
| β-strand | 173-175 | 3 | 21 |
| β-strand | 179-180 | 2 | 21 |
| β-strand | 186-195 | 10 | 21 |
| α-helix | 198-201 | 4 | |
| β-strand | 204-210 | 7 | 22 |
| α-helix | 211-213 | 3 | |
| β-strand | 215-221 | 7 | 22 |
Chain L: 9 helices, 21 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-7 | 4 | 12 |
| β-strand | 10-14 | 5 | 13 |
| β-strand | 19-25 | 7 | 12 |
| β-strand | 33-38 | 6 | 13 |
| β-strand | 45-49 | 5 | 13 |
| β-strand | 53-54 | 2 | 13 |
| α-helix | 55 | 1 | |
| β-strand | 62-67 | 6 | 12 |
| β-strand | 70-75 | 6 | 12 |
| α-helix | 80-82 | 3 | |
| β-strand | 84-90 | 7 | 13 |
| α-helix | 96 | 1 | |
| β-strand | 97-98 | 2 | 13 |
| β-strand | 102-107 | 6 | 13 |
| β-strand | 111 | 1 | 14 |
| α-helix | 112-113 | 2 | |
| β-strand | 114-118 | 5 | 15 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-126 | 5 | |
| β-strand | 129-139 | 11 | 15 |
| β-strand | 140 | 1 | 14 |
| β-strand | 145-150 | 6 | 16 |
| β-strand | 153-154 | 2 | 16 |
| α-helix | 155 | 1 | |
| β-strand | 159-163 | 5 | 15 |
| α-helix | 164-167 | 4 | |
| β-strand | 173-182 | 10 | 15 |
| α-helix | 183-187 | 5 | |
| β-strand | 191-197 | 7 | 16 |
| β-strand | 205-210 | 6 | 16 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Avastin Light Chain Fab fragment mutant | B, L | protein | 214 | Homo sapiens | Q8TCD0 (AlphaFold model) |
| Avastin Heavy Chain Fab fragment mutant | A, H | protein | 231 | Homo sapiens | P0DOX5 (AlphaFold model) |
| Vascular endothelial growth factor A | C, G | protein | 102 | Homo sapiens | P15692 (AlphaFold model) |
Sequence of entity 1 (B, L), FASTA
>6BFT_1 Avastin Light Chain Fab fragment mutant (chains B, L)
DIQMTQSPSSLSASVGDRVTITCSASQDISNYLNWYQQKPGKAPKVLIYFTDDLHSGVPS
RFSGSGSGTDFTLTISSLQPEDFATYYCQQYSTVPWTFGQGTKVEIKRTVAAPSVFIFPP
SDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLT
LSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
Sequence of entity 2 (A, H), FASTA
>6BFT_2 Avastin Heavy Chain Fab fragment mutant (chains A, H)
EVQLVESGGGLVQPGGSLRLSCAASGYDFDNYGMNWVRQAPGKGLEWVGWINTYTGEPTY
AADFKRRFTFSLDTSKSTAYLQMNSLRAEDTAVYYCAKYPHYYGSSHWYFDVWGQGTLVT
VSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVL
QSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHT
Sequence of entity 3 (C, G), FASTA
>6BFT_3 Vascular endothelial growth factor A (chains C, G)
GPNHHEVVKFMDVYQRSYCHPIETLVDIFQEYPDEIEYIFKPSCVPLMRCGGCCNDEGLE
CVPTEESNITMQIMRIKPHQGQHIGEMSFLQHNKCECRPKKD
Primary citation
Stable human IgG antibody therapeutics with native framework structure. Christie, M., Rouet, R., Nevoltris, D. et al. To be published.
Other PDB entries of the same protein (UniProt Q8TCD0 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 4NWU 1.6 Å, Crystal structure of APE1551, an anti-human NGF Fab with a nine amino acid insertion in…
- 6ARP 1.7 Å, Structure of a mutant Cetuximab Fab fragment
- 6DC4 1.7 Å, RSV-neutralizing human antibody AM22
- 4NWT 1.75 Å, Crystal structure of the anti-human NGF Fab APE1531
- 6UC5 1.75 Å, Fab397 in complex with NPNA peptide
- 3MNZ 1.8 Å, Crystal structure of the non-neutralizing HIV antibody 13H11 Fab fragment with a gp41…
- 4NUJ 1.83 Å, Crystal structure of HIV-1 broadly neutralizing antibody PGT152
- 4NUG 1.86 Å, Crystal structure of HIV-1 broadly neutralizing antibody PGT151
- 5VKK 2.01 Å, Crystal structure of Fab fragment of anti-CD22 Epratuzumab
- 3PGF 2.1 Å, Crystal structure of maltose bound MBP with a conformationally specific synthetic…
- 3MNW 2.2 Å, Crystal structure of the non-neutralizing HIV antibody 13H11 Fab fragment with a gp41…
- 6E4X 2.25 Å, Human antibody S5V2-29 in complex with influenza hemagglutinin A/Texas/50/2012 (H3N2)
Browse structure collections
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