MolNFT v1 · #107123 · protein
Crystal structure of M. tuberculosis CLPP1P1
4U0H · ATP-dependent clp protease proteolytic subunit 1: “Crystal structure of M. tuberculosis CLPP1P1”. X-ray diffraction, 1 ligand (SO4), 20 pockets (best druggability 0.58). MolNFT v1 #107123 on GenesisL1: 3D structure, binding sites…
- PDB
- 4U0H
- Type
- protein
- Length
- 1,232 residues
- Chains
- 7
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP-dependent clp protease proteolytic subunit 1
- EC
- 3.4.21.92
- UniProt
- P9WPC5
- Ligands
- SO4
- Pockets
- 20 · best druggability 0.58
Structure
x-ray diffraction · 7 distinct chains · 49% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent clp protease proteolytic subunit 1 (EC 3.4.21.92) | protein | 178 | 49% helix, 19% strand | P9WPC5 |
| B | ATP-dependent clp protease proteolytic subunit 1 (EC 3.4.21.92) | protein | 175 | 50% helix, 19% strand | P9WPC5 |
| C | ATP-dependent clp protease proteolytic subunit 1 (EC 3.4.21.92) | protein | 176 | 49% helix, 19% strand | P9WPC5 |
| D | ATP-dependent clp protease proteolytic subunit 1 (EC 3.4.21.92) | protein | 177 | 49% helix, 19% strand | P9WPC5 |
| E | ATP-dependent clp protease proteolytic subunit 1 (EC 3.4.21.92) | protein | 178 | 49% helix, 19% strand | P9WPC5 |
| F | ATP-dependent clp protease proteolytic subunit 1 (EC 3.4.21.92) | protein | 174 | 50% helix, 19% strand | P9WPC5 |
| G | ATP-dependent clp protease proteolytic subunit 1 (EC 3.4.21.92) | protein | 174 | 50% helix, 19% strand | P9WPC5 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 14 copies · chains A, B, C, D, E, G
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 167 | 0.58 | 0.82 | 21 | empty |
| 2 | 130 | 0.58 | 0.84 | 19 | empty |
| 3 | 170 | 0.58 | 0.81 | 27 | empty |
| 4 | 154 | 0.57 | 0.82 | 24 | empty |
| 5 | 169 | 0.56 | 0.81 | 21 | empty |
Interfaces
7 interfaces between chains.
- C–D · 1552 Ų buried · 16 hydrogen bonds · protein-protein
- A–G · 1494 Ų buried · 12 hydrogen bonds · protein-protein
- A–B · 1461 Ų buried · 14 hydrogen bonds · protein-protein
- E–F · 1436 Ų buried · 13 hydrogen bonds · protein-protein
- D–E · 1434 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 49 modified (engineered).
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 P9WPC5
- Elsewhere: RCSB PDB 4U0H · PDBe 4U0H · UniProt P9WPC5
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.