4B9K: Transcription elongation factor B polypeptide 2
pVHL-ELOB-ELOC complex_(2S,4R)-1-(3-amino-2-methylbenzoyl)-4-hydroxy-N-(4-(4-methylthiazol-5-yl)benzyl)pyrrolidine-2-carboxamide bound. Determined by X-ray diffraction at 2.0 Å resolution. Released 24 Oct 2012.
- Method
- X-ray diffraction
- Resolution
- 2.0 Å
- Organism
- HOMO SAPIENS
- Chains
- 12
- Atoms
- 11,711
- Mol. weight
- 173.73 kDa
- Ligands
- TG0
- Released
- 24 Oct 2012
Explore 4B9K in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
4B9K contains 71 α-helices and 106 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: 7 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-9 | 8 | 1 |
| β-strand | 10 | 1 | 2 |
| β-strand | 12-19 | 8 | 1 |
| β-strand | 23 | 1 | 3 |
| α-helix | 24-35 | 12 | |
| α-helix | 39-41 | 3 | |
| β-strand | 42-46 | 5 | 1 |
| β-strand | 49-50 | 2 | 1 |
| α-helix | 51-52 | 2 | |
| β-strand | 56 | 1 | 3 |
| β-strand | 68 | 1 | 4 |
| β-strand | 71 | 1 | 4 |
| α-helix | 72 | 1 | |
| β-strand | 73-79 | 7 | 1 |
| β-strand | 80 | 1 | 5 |
| β-strand | 85 | 1 | 5 |
| α-helix | 86-88 | 3 | |
| β-strand | 90 | 1 | 2 |
| α-helix | 91-100 | 10 | |
| α-helix | 101-103 | 3 | |
Chain B: 5 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 18-22 | 5 | 1 |
| β-strand | 28-32 | 5 | 1 |
| α-helix | 33-36 | 4 | |
| α-helix | 40-46 | 7 | |
| β-strand | 59-61 | 3 | 1 |
| α-helix | 67-83 | 17 | |
| α-helix | 90-94 | 5 | |
| α-helix | 100-110 | 11 | |
Chain C: 6 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 71-78 | 8 | 6 |
| α-helix | 83 | 1 | |
| β-strand | 84-89 | 6 | 7 |
| β-strand | 95-97 | 3 | 7 |
| β-strand | 101 | 1 | 7 |
| β-strand | 106-112 | 7 | 6 |
| β-strand | 116-121 | 6 | 7 |
| β-strand | 127 | 1 | 7 |
| β-strand | 129-130 | 2 | 6 |
| β-strand | 133 | 1 | 6 |
| β-strand | 136 | 1 | 7 |
| α-helix | 146 | 1 | |
| β-strand | 147-152 | 6 | 6 |
| α-helix | 158-169 | 12 | |
| α-helix | 172-177 | 6 | |
| α-helix | 182-189 | 8 | |
| α-helix | 194-198 | 5 | |
Chain D: 6 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-9 | 8 | 8 |
| β-strand | 10 | 1 | 9 |
| β-strand | 12-19 | 8 | 8 |
| β-strand | 23 | 1 | 10 |
| α-helix | 24-35 | 12 | |
| α-helix | 39-41 | 3 | |
| β-strand | 42-46 | 5 | 8 |
| β-strand | 49-50 | 2 | 8 |
| α-helix | 51-52 | 2 | |
| β-strand | 56 | 1 | 10 |
| β-strand | 68 | 1 | 11 |
| β-strand | 71 | 1 | 11 |
| α-helix | 72 | 1 | |
| β-strand | 73-79 | 7 | 8 |
| α-helix | 85-88 | 4 | |
| β-strand | 90 | 1 | 9 |
| α-helix | 91-99 | 9 | |
Chain E: 5 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 18-22 | 5 | 8 |
| β-strand | 28-32 | 5 | 8 |
| α-helix | 33-36 | 4 | |
| α-helix | 40-45 | 6 | |
| β-strand | 59-61 | 3 | 8 |
| α-helix | 67-83 | 17 | |
| α-helix | 89-94 | 6 | |
| α-helix | 100-110 | 11 | |
Chain F: 7 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 71-78 | 8 | 12 |
| α-helix | 83 | 1 | |
| β-strand | 84-89 | 6 | 13 |
| β-strand | 95-97 | 3 | 13 |
| β-strand | 101 | 1 | 13 |
| β-strand | 106-112 | 7 | 12 |
| β-strand | 116-121 | 6 | 13 |
| β-strand | 127 | 1 | 13 |
| β-strand | 129-130 | 2 | 12 |
| β-strand | 133 | 1 | 12 |
| β-strand | 136 | 1 | 13 |
| α-helix | 142-144 | 3 | |
| α-helix | 145-146 | 2 | |
| β-strand | 147-152 | 6 | 12 |
| α-helix | 158-169 | 12 | |
| α-helix | 172-177 | 6 | |
| α-helix | 182-189 | 8 | |
| α-helix | 194-202 | 9 | |
Chains G and J: 6 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-9 | 8 | 14 |
| β-strand | 10 | 1 | 15 |
| β-strand | 12-19 | 8 | 14 |
| β-strand | 23 | 1 | 16 |
| α-helix | 24-35 | 12 | |
| α-helix | 39-41 | 3 | |
| β-strand | 42-46 | 5 | 14 |
| β-strand | 49-50 | 2 | 14 |
| α-helix | 51-52 | 2 | |
| β-strand | 56 | 1 | 16 |
| β-strand | 68 | 1 | 17 |
| β-strand | 71 | 1 | 17 |
| α-helix | 72 | 1 | |
| β-strand | 73-79 | 7 | 14 |
| β-strand | 80-81 | 2 | 18 |
| β-strand | 84-85 | 2 | 18 |
| α-helix | 86-88 | 3 | |
| β-strand | 90 | 1 | 15 |
| α-helix | 91-100 | 10 | |
Chain H: 5 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 18-22 | 5 | 14 |
| β-strand | 28-32 | 5 | 14 |
| α-helix | 33-36 | 4 | |
| α-helix | 40-47 | 8 | |
| β-strand | 59-61 | 3 | 14 |
| α-helix | 67-83 | 17 | |
| α-helix | 90-94 | 5 | |
| α-helix | 97-110 | 14 | |
3 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 |
|---|
| Transcription elongation factor B polypeptide 2 | A, D, G, J | protein | 104 | HOMO SAPIENS | Q15370 (AlphaFold model) |
| Transcription elongation factor B polypeptide 1 | B, H, K | protein | 97 | HOMO SAPIENS | Q15369 (AlphaFold model) |
| Von hippel-lindau disease tumor suppressor | C, F, I, L | protein | 171 | HOMO SAPIENS | P40337 (AlphaFold model) |
| Transcription elongation factor B polypeptide 1 | E | protein | 97 | HOMO SAPIENS | Q15369 (AlphaFold model) |
Sequence of entity 1 (A, D, G, J), FASTA
>4B9K_1 TRANSCRIPTION ELONGATION FACTOR B POLYPEPTIDE 2 (chains A, D, G, J)
MDVFLMIRRHKTTIFTDAKESSTVFELKRIVEGILKRPPDEQRLYKDDQLLDDGKTLGEC
GFTSQTARPQAPATVGLAFRADDTFEALCIEPFSSPPELPDVMK
Sequence of entity 2 (B, H, K), FASTA
>4B9K_2 TRANSCRIPTION ELONGATION FACTOR B POLYPEPTIDE 1 (chains B, H, K)
MMYVKLISSDGHEFIVKREHALTSGTIKAMLSGPGQFAENETNEVNFREIPSHVLSKVCM
YFTYKVRYTNSSTEIPEFPIAPEIALELLMAANFLDC
Sequence of entity 3 (C, F, I, L), FASTA
>4B9K_3 VON HIPPEL-LINDAU DISEASE TUMOR SUPPRESSOR (chains C, F, I, L)
SMSENLYFQGSMEAGRPRPVLRSVNSREPSQVIFCNRSPRVVLPVWLNFDGEPQPYPTLP
PGTGRRIHSYRGHLWLFRDAGTHDGLLVNQTELFVPSLNVDGQPIFANITLPVYTLKERC
LQVVRSLVKPENYRRLDIVRSLYEDLEDHPNVQKDLERLTQERIAHQRMGD
Sequence of entity 4 (E), FASTA
>4B9K_4 TRANSCRIPTION ELONGATION FACTOR B POLYPEPTIDE 1 (chains E)
MMYVKLISSDGHEFIVKREHALTSGTIKAMLSGPGQFAENETNEVNFREIPSHVLSKVCM
YFTYKVRYTNSSTEIPEFPIAPEIALELLMAANFLDC
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| TG0 | (2S,4R)-1-(3-amino-2-methylbenzoyl)-4-hydroxy-N-(4-(4-methylthiazol-5-yl)benzyl… | C24 H26 N4 O3 S | 4 |
Water and common crystallization additives (ACT) are not listed.
Primary citation
Small-Molecule Inhibitors of the Interaction between the E3 Ligase Vhl and Hif1 Alpha. Buckley, D.L., Gustafson, J.L., Van Molle, I. et al. Angew Chem Int Ed Engl (2012) 51:11463. DOI 10.1002/ANIE.201206231 · PubMed
Other PDB entries of the same protein (UniProt Q15370 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 7Z76 1.32 Å, Crystal structure of compound 10 in complex with the bromodomain of human SMARCA2 and…
- 9GIO 1.49 Å, Crystal structure of the VHL-EloC-EloB complex with a covalent compound bound to C77 of…
- 7JTO 1.7 Å, Crystal structure of Protac MS33 in complex with the WD repeat-containing protein 5 and…
- 8BDS 1.72 Å, Ternary complex between VCB, BRD4-BD1 and PROTAC 48
- 4AJY 1.73 Å, von Hippel-Lindau protein-ElonginB-ElonginC complex, bound to Hif1- alpha peptide
- 6GMR 1.75 Å, pVHL:EloB:EloC in complex with (4-(1H-pyrrol-1-yl)phenyl)methanol
- 6HR2 1.76 Å, Crystal structure of PROTAC 2 in complex with the bromodomain of human SMARCA4 and…
- 7ZLM 1.79 Å, Crystal structure of SOCS2:ElonginB:ElonginC in complex with compound MN551
- 6I7Q 1.8 Å, Structure of pVHL-elongin B-elongin C (VCB) in complex with hydroxylated-HIF-2alpha…
- 8BB3 1.8 Å, Structure of human WDR5 and pVHL:ElonginC:ElonginB bound to PROTAC with PEG linker…
- 6GFX 1.83 Å, pVHL:EloB:EloC in complex with modified HIF-1a CODD peptide containing…
- 1LM8 1.85 Å, Structure of a HIF-1a-pVHL-ElonginB-ElonginC Complex
Browse structure collections
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