6KZ0: HRV14 3C
HRV14 3C in complex with single chain antibody GGVV. Determined by X-ray diffraction at 2.4 Å resolution. Released 27 May 2020.
- Method
- X-ray diffraction
- Resolution
- 2.4 Å
- Organisms
- Human rhinovirus 14, Homo sapiens
- Chains
- 12
- Atoms
- 12,416
- Mol. weight
- 185.49 kDa
- Released
- 27 May 2020
Explore 6KZ0 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
6KZ0 contains 65 α-helices and 148 β-strands across 12 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: 9 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-13 | 12 | |
| β-strand | 15-20 | 6 | 1 |
| β-strand | 23-31 | 9 | 1 |
| β-strand | 32 | 1 | 2 |
| β-strand | 34-38 | 5 | 1 |
| α-helix | 39-41 | 3 | |
| β-strand | 46-49 | 4 | 1 |
| β-strand | 52-61 | 10 | 1 |
| β-strand | 72-78 | 7 | 1 |
| α-helix | 82 | 1 | |
| β-strand | 83 | 1 | 2 |
| α-helix | 84 | 1 | |
| α-helix | 87-89 | 3 | |
| β-strand | 90 | 1 | 3 |
| β-strand | 98-105 | 8 | 3 |
| β-strand | 108-120 | 13 | 3 |
| β-strand | 135-137 | 3 | 3 |
| α-helix | 141-142 | 2 | |
| α-helix | 148 | 1 | |
| β-strand | 149-152 | 4 | 3 |
| β-strand | 155-163 | 9 | 3 |
| β-strand | 168-172 | 5 | 3 |
| α-helix | 173 | 1 | |
| α-helix | 175-177 | 3 | |
Chain B: 3 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 7-8 | 2 | 4 |
| β-strand | 12-14 | 3 | 5 |
| β-strand | 20-25 | 6 | 4 |
| β-strand | 36-41 | 6 | 5 |
| β-strand | 47-54 | 8 | 5 |
| α-helix | 55-57 | 3 | |
| β-strand | 59-62 | 4 | 5 |
| α-helix | 64-66 | 3 | |
| β-strand | 70-75 | 6 | 4 |
| β-strand | 80-85 | 6 | 4 |
| α-helix | 90-92 | 3 | |
| β-strand | 94-101 | 8 | 5 |
| β-strand | 111-114 | 4 | 5 |
| β-strand | 118-122 | 5 | 5 |
Chains C, F, I and L: 4 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-7 | 4 | 6 |
| β-strand | 10-13 | 4 | 7 |
| β-strand | 19-25 | 7 | 6 |
| 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 | 84-90 | 7 | 7 |
| α-helix | 97 | 1 | |
| β-strand | 98 | 1 | 7 |
| α-helix | 99 | 1 | |
| β-strand | 102-106 | 5 | 7 |
Chain D: 6 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 1-13 | 13 | |
| β-strand | 15-20 | 6 | 8 |
| β-strand | 23-31 | 9 | 8 |
| β-strand | 32 | 1 | 9 |
| β-strand | 34-38 | 5 | 8 |
| α-helix | 39-41 | 3 | |
| β-strand | 46-49 | 4 | 8 |
| β-strand | 52-61 | 10 | 8 |
| β-strand | 72-77 | 6 | 8 |
| β-strand | 83 | 1 | 9 |
| α-helix | 87-89 | 3 | |
| β-strand | 90 | 1 | 10 |
| β-strand | 98-105 | 8 | 10 |
| β-strand | 108-120 | 13 | 10 |
| β-strand | 135-137 | 3 | 10 |
| α-helix | 148 | 1 | |
| β-strand | 149-152 | 4 | 10 |
| β-strand | 155-163 | 9 | 10 |
| β-strand | 168-172 | 5 | 10 |
| α-helix | 173 | 1 | |
| α-helix | 175-177 | 3 | |
Chain E: 4 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 7-8 | 2 | 11 |
| β-strand | 12-14 | 3 | 12 |
| β-strand | 20-25 | 6 | 11 |
| α-helix | 28-31 | 4 | |
| β-strand | 36-41 | 6 | 12 |
| β-strand | 47-54 | 8 | 12 |
| α-helix | 55-57 | 3 | |
| β-strand | 59-62 | 4 | 12 |
| α-helix | 64-66 | 3 | |
| β-strand | 70-75 | 6 | 11 |
| β-strand | 80-85 | 6 | 11 |
| α-helix | 90-92 | 3 | |
| β-strand | 94-101 | 8 | 12 |
| β-strand | 111-114 | 4 | 12 |
| β-strand | 118-122 | 5 | 12 |
Chain G: 9 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 1-13 | 13 | |
| β-strand | 15-20 | 6 | 15 |
| β-strand | 23-31 | 9 | 15 |
| β-strand | 32 | 1 | 16 |
| β-strand | 34-38 | 5 | 15 |
| α-helix | 39-41 | 3 | |
| β-strand | 46-49 | 4 | 15 |
| β-strand | 52-61 | 10 | 15 |
| β-strand | 72-78 | 7 | 15 |
| α-helix | 82 | 1 | |
| β-strand | 83 | 1 | 16 |
| α-helix | 84 | 1 | |
| α-helix | 87-89 | 3 | |
| β-strand | 90 | 1 | 17 |
| β-strand | 98-105 | 8 | 17 |
| β-strand | 108-119 | 12 | 17 |
| β-strand | 135-138 | 4 | 17 |
| α-helix | 141-142 | 2 | |
| α-helix | 148 | 1 | |
| β-strand | 149-152 | 4 | 17 |
| β-strand | 155-163 | 9 | 17 |
| β-strand | 167-172 | 6 | 17 |
| α-helix | 173 | 1 | |
| α-helix | 175-177 | 3 | |
Chain H: 5 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 7-8 | 2 | 18 |
| α-helix | 9 | 1 | |
| β-strand | 12-14 | 3 | 19 |
| β-strand | 20-25 | 6 | 18 |
| α-helix | 28-33 | 6 | |
| β-strand | 36-41 | 6 | 19 |
| β-strand | 47-54 | 8 | 19 |
| α-helix | 55-57 | 3 | |
| β-strand | 59-62 | 4 | 19 |
| α-helix | 64-66 | 3 | |
| β-strand | 70-75 | 6 | 18 |
| β-strand | 80-85 | 6 | 18 |
| α-helix | 90-92 | 3 | |
| β-strand | 94-101 | 8 | 19 |
| β-strand | 111-114 | 4 | 19 |
| β-strand | 118-122 | 5 | 19 |
Chain J: 9 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-13 | 12 | |
| β-strand | 15-20 | 6 | 22 |
| β-strand | 23-31 | 9 | 22 |
| β-strand | 32 | 1 | 23 |
| β-strand | 34-38 | 5 | 22 |
| α-helix | 39-41 | 3 | |
| β-strand | 46-49 | 4 | 22 |
| β-strand | 52-61 | 10 | 22 |
| β-strand | 72-77 | 6 | 22 |
| α-helix | 82 | 1 | |
| β-strand | 83 | 1 | 23 |
| α-helix | 84 | 1 | |
| α-helix | 87-89 | 3 | |
| β-strand | 90 | 1 | 24 |
| β-strand | 98-105 | 8 | 24 |
| β-strand | 108-120 | 13 | 24 |
| β-strand | 135-137 | 3 | 24 |
| α-helix | 141-142 | 2 | |
| α-helix | 148 | 1 | |
| β-strand | 149-152 | 4 | 24 |
| β-strand | 155-163 | 9 | 24 |
| β-strand | 168-172 | 5 | 24 |
| α-helix | 173 | 1 | |
| α-helix | 175-177 | 3 | |
1 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Genome polyprotein | A, D, G, J | protein | 184 | Human rhinovirus 14 | P03303 (AlphaFold model) |
| GGVV H chain | B, E, H, K | protein | 142 | Homo sapiens | |
| GGVV L chain | C, F, I, L | protein | 108 | Homo sapiens | |
Sequence of entity 1 (A, D, G, J), FASTA
>6KZ0_1 Genome polyprotein (chains A, D, G, J)
GSGPNTEFALSLLRKNIMTITTSKGEFTGLGIHDRVCVIPTHAQPGDDVLVNGQKIRVKD
KYKLVDPENINLELTVLTLDRNEKFRDIRGFISEDLEGVDATLVVHSNNFTNTILEVGPV
TMAGLINLSSTPTNRMIRYDYATKTGQCGGVLCATGKIFGIHVGGNGRQGFSAQLKKQYF
VEKQ
Sequence of entity 2 (B, E, H, K), FASTA
>6KZ0_2 GGVV H chain (chains B, E, H, K)
GAMMAQVQLVQSGAEVKQPGSSVKVSCKTSGDIFSTYGFNWVRQAPGQGLEWMGGIAPVF
DTLKYAQRFQGRLLITADESATSVYMELSSLRSDDTAVYYCARAGQGGVVGNYLDYWGQG
TLVTVSSGGGGSGGGGSGGGGS
Sequence of entity 3 (C, F, I, L), FASTA
>6KZ0_3 GGVV L chain (chains C, F, I, L)
DIQMTQSPSSLSASVGDRVTITCRASQGISNYLAWYQQKPGKVPKLLIYAASTLQSGVPS
RFSGSGSGTDFTLTISSLQPEDVATYYCQKYNSAPLTFGQGTKVDIKR
Primary citation
Inhibitory antibodies identify unique sites of therapeutic vulnerability in rhinovirus and other enteroviruses. Meng, B., Lan, K., Xie, J. et al. Proc Natl Acad Sci U S A (2020) 117:13499-13508. DOI 10.1073/pnas.1918844117 · PubMed
Other PDB entries of the same protein (UniProt P03303 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 6KYZ 1.84 Å, HRV14 3C in complex with single chain antibody YDF
- 9LGP 2.11 Å, Crystal structure of the HRV B14 3C protease in complex with AG7404
- 5W3M 2.26 Å, CryoEM structure of rhinovirus B14 in complex with C5 Fab (33 degrees Celsius, molar…
- 7BG7 2.4 Å, HRV14 in complex with its receptor ICAM-1
- 1NCQ 2.5 Å, The structure of HRV14 when complexed with pleconaril, an antiviral compound
- 5W3E 2.53 Å, CryoEM structure of rhinovirus B14 in complex with C5 Fab (33 degrees Celsius, molar…
- 7BG6 2.6 Å, HRV14 native particle solved by cryoEM
- 31LE 2.64 Å, HRV E1007A mutant
- 1K5M 2.7 Å, Crystal Structure of a Human Rhinovirus Type 14:Human Immunodeficiency Virus Type 1 V3…
- 31LF 2.71 Å, HRV virion E2250A mutant
- 5W3L 2.71 Å, CryoEM structure of rhinovirus B14 in complex with C5 Fab (4 degrees Celsius, molar…
- 29UB 2.73 Å, HRV B14 virion
Browse structure collections
About this viewer
MolViewer shows 6KZ0 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.