Research workbench
Protein farnesyltransferase complexed with a farnesylated ddptasacvls peptide product at 1.5A resolution
Analyse Protein farnesyltransferase complexed with a farnesylated ddptasacvls peptide… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2H6F
- Type
- protein
- Length
- 729 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein FARNESYLTRANSFERASE/GERANYLGERANYLTRANSFERASE type I alpha subunit; Protein…
- EC
- 2.5.1.58, 2.5.1.59
- UniProt
- P49354, P49356
- Ligands
- FAR, GLC, FRU, ZN
- Pockets
- 11 · best druggability 0.76
Structure
x-ray diffraction · 3 distinct chains · 58% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein FARNESYLTRANSFERASE/GERANYLGERANYLTRANSFERASE type I alpha subunit (EC 2.5.1.58, 2.5.1.59) | protein | 315 | 70% helix, 1% strand | P49354 |
| B | Protein farnesyltransferase beta subunit (EC 2.5.1.58) | protein | 410 | 50% helix, 7% strand | P49356 |
| P | Farnesylated peptide | protein | 4 | 0% helix, 0% strand | — |
Ligands and binding sites
- FAR · Farnesyl · ligand · chains A, B, P
- GLC · alpha-D-glucopyranose · sugar · chains A, B
- FRU · beta-D-fructofuranose · sugar · chains A, B
- ZN · Zinc ion · metal · chains B, P
- ACY · Acetic acid · additive · 5 copies · chains A, B, P
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 617 | 0.76 | 0.82 | 77 | ACY, FAR |
| 2 | 222 | 0.74 | 0.89 | 38 | empty |
| 3 | 320 | 0.72 | 0.85 | 47 | empty |
| 4 | 248 | 0.64 | 0.82 | 32 | ACY |
| 5 | 236 | 0.53 | 0.76 | 35 | empty |
Interfaces
3 interfaces between chains.
- A–B · 3499 Ų buried · 72 hydrogen bonds · protein-protein
- B–P · 284 Ų buried · 2 hydrogen bonds · protein-protein
- A–P · 123 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 1 lipid (farnesylation).
Compared structures
- 2H6F · Protein Farnesyltransferase Complexed with a Farnesylated DDPTASACVLS Peptide Product at… · the same entry in another collection · chain A against A, TM-score 1.00
- P49356 · AlphaFold monomer V2.0 prediction for protein farnesyltransferase subunit beta (P49356) · a predicted model of the same protein · chain B against A, TM-score 1.00
- P49354 · AlphaFold monomer V2.0 prediction for protein FARNESYLTRANSFERASE/GERANYLGERANYLTRANSFERAS… · a predicted model of the same protein · chain A against A, TM-score 0.99
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P49354
- Every structure of UniProt P49356
- Elsewhere: RCSB PDB 2H6F · PDBe 2H6F · UniProt P49354 · UniProt P49356
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.