MolNFT v1 · #118042 · protein
Pseudomonas aeruginosa pilm bound to AMP-pnp
5EQ6 · Type 4 fimbrial biogenesis protein pilm: “Pseudomonas aeruginosa pilm bound to AMP-pnp”. X-ray diffraction, 2 ligands (ANP, MG), 5 pockets (best druggability 0.77). MolNFT v1 #118042 on GenesisL1: 3D structure, binding sites and…
- PDB
- 5EQ6
- Type
- protein
- Length
- 709 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Type 4 fimbrial biogenesis protein pilm
- UniProt
- G3XD28
- Ligands
- ANP, MG
- Pockets
- 5 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Type 4 fimbrial biogenesis protein pilm | protein | 357 | 38% helix, 29% strand | G3XD28 |
| B | Type 4 fimbrial biogenesis protein pilm | protein | 352 | 41% helix, 29% strand | G3XD28 |
Ligands and binding sites
- ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 784 | 0.77 | 0.81 | 74 | ANP, MG |
| 2 | 642 | 0.74 | 0.80 | 68 | ANP, MG |
| 3 | 853 | 0.70 | 0.76 | 86 | empty |
| 4 | 75 | 0.37 | 0.77 | 18 | empty |
| 5 | 50 | 0.28 | 0.75 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 1513 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
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 G3XD28
- Elsewhere: RCSB PDB 5EQ6 · PDBe 5EQ6 · UniProt G3XD28
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