MolNFT v1 · #145526 · protein
High resolution crystal structure of ftsy-ng domain of E. COLI
6CQP · Signal recognition particle receptor ftsy: “High resolution crystal structure of ftsy-ng domain of E. COLI”. X-ray diffraction, 1 ligand (NA), 4 pockets (best druggability 0.82). MolNFT v1 #145526 on GenesisL1: 3D structure, binding…
- PDB
- 6CQP
- Type
- protein
- Length
- 604 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Signal recognition particle receptor ftsy
- UniProt
- P10121
- Ligands
- NA
- Pockets
- 4 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 53% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Signal recognition particle receptor ftsy | protein | 303 | 52% helix, 13% strand | P10121 |
| B | Signal recognition particle receptor ftsy | protein | 301 | 54% helix, 13% strand | P10121 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 651 | 0.82 | 0.86 | 55 | empty |
| 2 | 89 | 0.38 | 0.77 | 22 | NA |
| 3 | 86 | 0.32 | 0.74 | 17 | empty |
| 4 | 56 | 0.31 | 0.76 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 791 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 6CQP · High resolution crystal structure of FtsY-NG domain of E. coli · the same entry in another collection · chain A against A, TM-score 1.00
- P10121 · AlphaFold monomer V2.0 prediction for signal recognition particle receptor ftsy (P10121) · a predicted model of the same protein · chain B against A, TM-score 0.98
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 P10121
- Elsewhere: RCSB PDB 6CQP · PDBe 6CQP · UniProt P10121
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