cryo-EM structure of human rhinovirus 16 (HRV16) complexed with a two-domain fragment of its cellular receptor, intercellular adhesion molecule-1 (D1D2-icam-1). Implications for virus-receptor interactions. Alpha carbons only. Determined by electron microscopy at 28.0 Å resolution. Released 19 Jan 2000.
Explore 1D3E in 3D Show helices and sheets RCSB PDB PDBe
1D3E contains 12 α-helices and 44 β-strands across 5 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 66-72 | 7 | |
| β-strand | 75-83 | 9 | 11 |
| β-strand | 93-97 | 5 | 12 |
| α-helix | 98-101 | 4 | |
| α-helix | 104-110 | 7 | |
| β-strand | 112-130 | 19 | 11 |
| β-strand | 137-145 | 9 | 12 |
| α-helix | 158-162 | 5 | |
| β-strand | 165-171 | 7 | 12 |
| β-strand | 177-192 | 16 | 11 |
| β-strand | 216-221 | 6 | 12 |
| β-strand | 230-248 | 19 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 14-18 | 5 | 21 |
| β-strand | 21-25 | 5 | 21 |
| α-helix | 56-59 | 4 | |
| β-strand | 69-71 | 3 | 22 |
| β-strand | 78-82 | 5 | 23 |
| α-helix | 90-98 | 9 | |
| β-strand | 99-111 | 13 | 22 |
| β-strand | 119-128 | 10 | 23 |
| α-helix | 179-184 | 6 | |
| β-strand | 187-191 | 5 | 23 |
| β-strand | 196-202 | 7 | 22 |
| β-strand | 219-230 | 12 | 23 |
| β-strand | 238-254 | 17 | 22 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-6 | 5 | 31 |
| α-helix | 44-47 | 4 | |
| β-strand | 69-72 | 4 | 32 |
| β-strand | 78-87 | 10 | 33 |
| α-helix | 98-103 | 6 | |
| β-strand | 106-119 | 14 | 32 |
| β-strand | 128-134 | 7 | 33 |
| α-helix | 143-148 | 6 | |
| β-strand | 151-156 | 6 | 33 |
| β-strand | 162-167 | 6 | 32 |
| β-strand | 188-193 | 6 | 33 |
| β-strand | 207-224 | 18 | 32 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-6 | 5 | 41 |
| β-strand | 23-30 | 8 | 41 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-5 | 4 | 1 |
| β-strand | 8-12 | 5 | 2 |
| β-strand | 17-23 | 7 | 1 |
| β-strand | 30-34 | 5 | 3 |
| β-strand | 38-42 | 5 | 1 |
| β-strand | 49-55 | 7 | 1 |
| β-strand | 64-68 | 5 | 3 |
| β-strand | 73-77 | 5 | 3 |
| β-strand | 79-83 | 5 | 2 |
| β-strand | 88-91 | 4 | 4 |
| α-helix | 116-118 | 3 | |
| β-strand | 119-125 | 7 | 5 |
| β-strand | 128-134 | 7 | 5 |
| β-strand | 140-147 | 8 | 4 |
| β-strand | 157-164 | 8 | 5 |
| α-helix | 166-168 | 3 | |
| β-strand | 172-176 | 5 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein (intercellular adhesion molecule-1) | I | protein | 185 | Homo sapiens | P05362 (AlphaFold model) |
| Protein (rhinovirus 16 coat protein VP1) | 1 | protein | 285 | Human rhinovirus sp. | Q82122 (AlphaFold model) |
| Protein (rhinovirus 16 coat protein VP2) | 2 | protein | 252 | Human rhinovirus sp. | Q82122 (AlphaFold model) |
| Protein (rhinovirus 16 coat protein VP3) | 3 | protein | 238 | Human rhinovirus sp. | Q82122 (AlphaFold model) |
| Protein (rhinovirus 16 coat protein VP4) | 4 | protein | 68 | Human rhinovirus sp. | Q82122 (AlphaFold model) |
>1D3E_1 PROTEIN (INTERCELLULAR ADHESION MOLECULE-1) (chains I) QTSVSPSKVILPRGGSVLVTCSTSCDQPKLLGIETPLPKKELLLPGNNRKVYELSNVQED SQPMCYSNCPDGQSTAKTFLTVYWTPERVELAPLPSWQPVGKNLTLRCQVEGGAPRANLT VVLLRGEKELKREPAVGEPAEVTTTVLVRRDHHGANFSCRTELDLRPQGLELFENTSAPY QLQTF
>1D3E_2 PROTEIN (RHINOVIRUS 16 COAT PROTEIN VP1) (chains 1) APVAAYVDEVLNEVLVVPNINQSHPTTSNAAPVLDAAETGHTNKIQPEDTIETRYVQSSQ TLDEMSVESFLGRSGCIHESVLDIVDNYNDQSFTKWNINLQEMAQIRRKFEMFTYARFDS EITMVPSVAAKDGHIGHIVMQYMYVPPGAPIPTTRDDYAWQSGTNASVFWQHGQPFPRFS LPFLSIASAYYMFYDGYDGDTYKSRYGTVVTNDMGTLCSRIVTSEQLHKVKVVTRIYHKA KHTKAWCPRPPRAVQYSHTHTTNYKLSSEVHNDVAIRPRTNLTTV
>1D3E_3 PROTEIN (RHINOVIRUS 16 COAT PROTEIN VP2) (chains 2) SDRIIQITRGDSTITSQDVANAVVGYGVWPHYLTPQDATAIDKPTQPDTSSNRFYTLDSK MWNSTSKGWWWKLPDALKDMGIFGENMFYHFLGRSGYTVHVQCNASKFHQGTLLVVMIPE HQLATVNKGNVNAGYKYTHPGEAGREVGTAAAAEKQPSDDNWLNFDGTLLGNLLIFPHQF INLRSNNSATLIVPYVNAVPMDSMVRHNNWSLVIIPVCQLQSNNISNIVPITVSISPMCA EFSGARAKTVVQ
>1D3E_4 PROTEIN (RHINOVIRUS 16 COAT PROTEIN VP3) (chains 3) GLPVYVTPGSGQFMTTDDMQSPCALPWYHPTKEIFIPGEVKNLIEMCQVDTLIPINSTQS NIGNVSMYTVTLSPQTKLAEEIFAIKVDIASHPLATTLIGEIASYFTHWTGSLRFSFMFC GTANTTLKVLLAYTPPGIGKPRSRKEAMLGTHVVWDVGLQSTVSLVVPWISASQYRFTTP DTYSSAGYITCWYQTNFVVPPNTPNTAEMLCFVSGCKDFCLRMARDTDLHKQTGPITQ
>1D3E_5 PROTEIN (RHINOVIRUS 16 COAT PROTEIN VP4) (chains 4) GAQVSRQNVGTHSTQNMVSNGSSLNYFNINYFKDAASSGASRLDFSQDPSKFTDPVKDVL EKGIPTLQ
Structural studies of two rhinovirus serotypes complexed with fragments of their cellular receptor. Kolatkar, P.R., Bella, J., Olson, N.H. et al. EMBO J (1999) 18:6249-6259. DOI 10.1093/emboj/18.22.6249 · PubMed
Other PDB entries of the same protein (UniProt P05362 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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