5TUD: PDB entry 5TUD
Structural Insights into the Extracellular Recognition of the Human Serotonin 2B Receptor by an Antibody. Determined by X-ray diffraction at 3.0 Å resolution. Released 26 Jul 2017.
- Method
- X-ray diffraction
- Resolution
- 3.0 Å
- Organisms
- Homo sapiens, Escherichia coli, Mus musculus
- Chains
- 6
- Atoms
- 12,395
- Mol. weight
- 201.43 kDa
- Ligands
- ERM
- Released
- 26 Jul 2017
Explore 5TUD in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
5TUD contains 58 α-helices and 99 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: 17 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 57-81 | 25 | |
| α-helix | 88-102 | 15 | |
| α-helix | 103-107 | 5 | |
| α-helix | 108-116 | 9 | |
| α-helix | 127-158 | 32 | |
| α-helix | 168-187 | 20 | |
| α-helix | 189-192 | 4 | |
| β-strand | 195-197 | 3 | 1 |
| α-helix | 202-204 | 3 | |
| α-helix | 215-222 | 8 | |
| α-helix | 223-227 | 5 | |
| α-helix | 228-1016 | 37 | |
| α-helix | 1023-1040 | 18 | |
| α-helix | 1059-1080 | 22 | |
| α-helix | 1084-336 | 46 | |
| α-helix | 338-349 | 12 | |
| α-helix | 355-379 | 25 | |
| α-helix | 385-395 | 11 | |
Chain B: 6 helices, 24 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-5 | 2 | 2 |
| β-strand | 10-13 | 4 | 3 |
| β-strand | 20-25 | 6 | 2 |
| β-strand | 33-37 | 5 | 3 |
| β-strand | 44-48 | 5 | 3 |
| β-strand | 52-53 | 2 | 3 |
| β-strand | 61-65 | 5 | 2 |
| β-strand | 69-74 | 6 | 2 |
| α-helix | 79-81 | 3 | |
| β-strand | 84-88 | 5 | 3 |
| α-helix | 95 | 1 | |
| β-strand | 96 | 1 | 4 |
| β-strand | 97 | 1 | 3 |
| β-strand | 98 | 1 | 2 |
| β-strand | 102-105 | 4 | 3 |
| β-strand | 110 | 1 | 5 |
| β-strand | 113-117 | 5 | 6 |
| α-helix | 118-120 | 3 | |
| α-helix | 121-124 | 4 | |
| β-strand | 128-138 | 11 | 6 |
| β-strand | 139 | 1 | 5 |
| β-strand | 144-149 | 6 | 7 |
| β-strand | 153 | 1 | 7 |
| β-strand | 158-162 | 5 | 6 |
| α-helix | 163-166 | 4 | |
| β-strand | 172-181 | 10 | 6 |
| α-helix | 182-185 | 4 | |
| β-strand | 190-196 | 7 | 7 |
| β-strand | 204-205 | 2 | 7 |
| β-strand | 208-209 | 2 | 7 |
Chain C: 5 helices, 25 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-6 | 4 | 8 |
| β-strand | 10-12 | 3 | 9 |
| β-strand | 18-25 | 8 | 8 |
| β-strand | 34-40 | 7 | 4 |
| β-strand | 44-51 | 8 | 4 |
| β-strand | 58-60 | 3 | 4 |
| β-strand | 68-73 | 6 | 8 |
| β-strand | 78-83 | 6 | 8 |
| β-strand | 93-98 | 6 | 4 |
| β-strand | 102-104 | 3 | 1 |
| β-strand | 109-111 | 3 | 1 |
| β-strand | 116-117 | 2 | 4 |
| α-helix | 118-120 | 3 | |
| β-strand | 121-122 | 2 | 4 |
| β-strand | 123-125 | 3 | 9 |
| α-helix | 129-130 | 2 | |
| β-strand | 134-138 | 5 | 10 |
| β-strand | 150-157 | 8 | 10 |
| β-strand | 159 | 1 | 11 |
| β-strand | 164-168 | 5 | 12 |
| β-strand | 173 | 1 | 12 |
| β-strand | 177-179 | 3 | 10 |
| α-helix | 180-182 | 3 | |
| β-strand | 183-184 | 2 | 11 |
| β-strand | 190-191 | 2 | 11 |
| β-strand | 193-198 | 6 | 10 |
| α-helix | 202-205 | 4 | |
| β-strand | 209-214 | 6 | 12 |
| β-strand | 219-224 | 6 | 12 |
| α-helix | 227-230 | 4 | |
Chain D: 18 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 56-81 | 26 | |
| α-helix | 83-85 | 3 | |
| α-helix | 88-102 | 15 | |
| α-helix | 103-107 | 5 | |
| α-helix | 108-116 | 9 | |
| α-helix | 127-158 | 32 | |
| α-helix | 168-187 | 20 | |
| α-helix | 189-192 | 4 | |
| β-strand | 195-197 | 3 | 13 |
| α-helix | 202-204 | 3 | |
| α-helix | 215-222 | 8 | |
| α-helix | 223-227 | 5 | |
| α-helix | 228-1017 | 38 | |
| α-helix | 1023-1043 | 21 | |
| α-helix | 1060-1080 | 21 | |
| α-helix | 1084-336 | 46 | |
| α-helix | 338-349 | 12 | |
| α-helix | 355-379 | 25 | |
| α-helix | 385-395 | 11 | |
Chain E: 7 helices, 22 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-7 | 4 | 14 |
| β-strand | 10-13 | 4 | 15 |
| β-strand | 19-25 | 7 | 14 |
| β-strand | 33-37 | 5 | 15 |
| β-strand | 44-49 | 6 | 15 |
| β-strand | 52-53 | 2 | 15 |
| β-strand | 61-65 | 5 | 14 |
| β-strand | 69-74 | 6 | 14 |
| α-helix | 79-81 | 3 | |
| β-strand | 84-89 | 6 | 15 |
| α-helix | 95 | 1 | |
| β-strand | 96-97 | 2 | 15 |
| β-strand | 98 | 1 | 14 |
| β-strand | 101-105 | 5 | 15 |
| β-strand | 110 | 1 | 16 |
| β-strand | 113-117 | 5 | 17 |
| α-helix | 118-120 | 3 | |
| α-helix | 121-124 | 4 | |
| β-strand | 128-138 | 11 | 17 |
| β-strand | 139 | 1 | 16 |
| β-strand | 144-149 | 6 | 18 |
| β-strand | 152-153 | 2 | 18 |
| α-helix | 154 | 1 | |
| β-strand | 158-162 | 5 | 17 |
| α-helix | 163-166 | 4 | |
| β-strand | 172-181 | 10 | 17 |
| α-helix | 182-185 | 4 | |
| β-strand | 190-196 | 7 | 18 |
| β-strand | 204-209 | 6 | 18 |
Chain F: 5 helices, 26 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-6 | 4 | 19 |
| α-helix | 7-9 | 3 | |
| β-strand | 10-12 | 3 | 20 |
| β-strand | 18-20 | 3 | 19 |
| β-strand | 22-25 | 4 | 19 |
| β-strand | 34-40 | 7 | 21 |
| β-strand | 44-51 | 8 | 21 |
| β-strand | 58-60 | 3 | 21 |
| β-strand | 68-73 | 6 | 19 |
| β-strand | 78-83 | 6 | 19 |
| β-strand | 93-98 | 6 | 21 |
| β-strand | 102-104 | 3 | 13 |
| β-strand | 109-111 | 3 | 13 |
| β-strand | 116-117 | 2 | 21 |
| α-helix | 118-120 | 3 | |
| β-strand | 121-122 | 2 | 21 |
| β-strand | 123-125 | 3 | 20 |
| α-helix | 129-130 | 2 | |
| β-strand | 131 | 1 | 22 |
| β-strand | 134-137 | 4 | 23 |
| α-helix | 142-144 | 3 | |
| β-strand | 149-157 | 9 | 23 |
| β-strand | 159 | 1 | 23 |
| β-strand | 160 | 1 | 22 |
| β-strand | 164-168 | 5 | 24 |
| β-strand | 173 | 1 | 24 |
| β-strand | 177-184 | 8 | 23 |
| β-strand | 190-199 | 10 | 23 |
| α-helix | 202-205 | 4 | |
| β-strand | 209-214 | 6 | 24 |
| β-strand | 219-224 | 6 | 24 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| 5-hydroxytryptamine receptor 2B,Soluble cytochrome b562 chimera | A, D | protein | 457 | Homo sapiens, Escherichia coli | P0ABE7 (AlphaFold model), P41595 (AlphaFold model) |
| Anti-5-HT2B Fab light chain | B, E | protein | 213 | Mus musculus | |
| Anti-5-HT2B Fab heavy chain | C, F | protein | 236 | Mus musculus | |
Sequence of entity 1 (A, D), FASTA
>5TUD_1 5-hydroxytryptamine receptor 2B,Soluble cytochrome b562 chimera (chains A, D)
MKTIIALSYIFCLVFADYKDDDDGAPTESIPEEMKQIVEEQGNKLHWAALLILMVIIPTI
GGNTLVILAVSLEKKLQYATNYFLMSLAVADLLVGLFVMPIALLTIMFEAMWPLPLVLCP
AWLFLDVLFSTASIWHLCAISVDRYIAIKKPIQANQYNSRATAFIKITVVWLISIGIAIP
VPIKGIETDVDNPNNITCVLTKERFGDFMLFGSLAAFFTPLAIMIVTYFLTIHALQKKAA
DLEDNWETLNDNLKVIEKADNAAQVKDALTKMRAAALDAQKATPPKLEDKSPDSPEMKDF
RHGFDILVGQIDDALKLANEGKVKEAQAAAEQLKTTRNAYIQKYLQTISNEQRASKVLGI
VFFLFLLMWCPFFITNITLVLCDSCNQTTLQMLLEIFVWIGYVSSGVNPLVYTLFNKTFR
DAFGRYITCNYRATKSVGRPLEVLFQGPHHHHHHHHH
Sequence of entity 2 (B, E), FASTA
>5TUD_2 Anti-5-HT2B Fab light chain (chains B, E)
DIVLIQSPAIMSASPGEKVTITCSASSSVSYMHWFQQKPGTSPKLWIYSTSNLASGVPAR
FSGSGSGTSYSLTISRMEAEDAATYYCQQRSSYPLTFGAGTKLEIKRTVAAPSVFIFPPS
DEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTL
SKADYEKHKVYACEVTHQGLSLPVTKSFNRGEC
Sequence of entity 3 (C, F), FASTA
>5TUD_3 Anti-5-HT2B Fab heavy chain (chains C, F)
EVQLQQSGPELVKPGASVKLSCKASGYTFTSSWMHWVKQRPGQGLEWIGNIYPSNGGTNY
NERFKSKATLTVDRSSNTAYMQLSSLTSEDSAVYFCARFGSFITTILTTYYNPVDYWGQG
TTLTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTF
PAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCHHHHHH
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| ERM | Ergotamine | C33 H35 N5 O5 | 2 |
Primary citation
Structural insights into the extracellular recognition of the human serotonin 2B receptor by an antibody. Ishchenko, A., Wacker, D., Kapoor, M. et al. Proc Natl Acad Sci U S A (2017) 114:8223-8228. DOI 10.1073/pnas.1700891114 · PubMed
Other PDB entries of the same protein (UniProt P0ABE7 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 6DYF 1.1 Å, Cu(II)-bound structure of the engineered cyt cb562 variant, CH3Y
- 5YO6 1.2 Å, Crystal Structure of B562RIL with engineered disulfide bond T9C-A36C
- 4JEA 1.22 Å, Crystal structure of an engineered Zn-RIDC1 construct with four interfacial disulfide…
- 7LSJ 1.26 Å, Cu-bound crystal structure of the engineered cyt cb562 variant, DiCyt2 - H63A,…
- 7MK4 1.27 Å, Co-bound crystal structure of the engineered cyt cb562 variant, DiCyt2
- 6DYC 1.33 Å, Co(II)-bound structure of the engineered cyt cb562 variant, CH3
- 5YO4 1.37 Å, Crystal Structure of B562RIL with engineered disulfide bond K27C-A79C
- 256B 1.4 Å, Improvement of the 2.5 Å resolution model of cytochrome B562 by redetermining the…
- 6OT4 1.4 Å, Bimetallic dodecameric cage design 2 (BMC2) from cytochrome cb562
- 7LRV 1.4 Å, Ni-bound crystal structure of the engineered cyt cb562 variant, DiCyt2, crystallized in…
- 9PQ4 1.48 Å, Bi-bound structure of the H77C variant of TriCyt2
- 6DYG 1.49 Å, Fe(II)-bound structure of the engineered cyt cb562 variant, CH3Y
Browse structure collections
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