MolNFT v1 · #20827 · protein
Catalytic domain of E.COLI lon protease
1RR9 · ATP-dependent protease la: “Catalytic domain of E.COLI lon protease”. X-ray diffraction, 1 ligand (SO4), 13 pockets (best druggability 0.56). MolNFT v1 #20827 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1RR9
- Type
- protein
- Length
- 1,101 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP-dependent protease la
- EC
- 3.4.21.53
- UniProt
- P0A9M0
- Ligands
- SO4
- Pockets
- 13 · best druggability 0.56
Structure
x-ray diffraction · 3 distinct chains · 36% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | ATP-dependent protease la (EC 3.4.21.53) | protein | 182 | 35% helix, 30% strand | P0A9M0 |
| E | ATP-dependent protease la (EC 3.4.21.53) | protein | 191 | 35% helix, 26% strand | P0A9M0 |
| F | ATP-dependent protease la (EC 3.4.21.53) | protein | 182 | 38% helix, 29% strand | P0A9M0 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 5 copies · chains B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 117 | 0.56 | 0.83 | 22 | empty |
| 2 | 141 | 0.54 | 0.81 | 28 | empty |
| 3 | 63 | 0.50 | 0.85 | 15 | empty |
| 4 | 93 | 0.48 | 0.81 | 17 | empty |
| 5 | 128 | 0.47 | 0.79 | 25 | empty |
Interfaces
6 interfaces between chains.
- A–F · 832 Ų buried · 13 hydrogen bonds · protein-protein
- C–D · 777 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 757 Ų buried · 12 hydrogen bonds · protein-protein
- E–F · 751 Ų buried · 7 hydrogen bonds · protein-protein
- B–C · 746 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
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 P0A9M0
- Elsewhere: RCSB PDB 1RR9 · PDBe 1RR9 · UniProt P0A9M0
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