MolNFT v1 · #66279 · protein
Crystal structure of clpp A153C mutant with inter-heptamer disulfide bonds
3HLN · ATP-dependent clp protease proteolytic subunit: “Crystal structure of clpp A153C mutant with inter-heptamer disulfide bonds”. X-ray diffraction, 1 ligand (CA), 20 pockets (best druggability 0.87). MolNFT v1 #66279 on GenesisL1: 3D…
- PDB
- 3HLN
- Type
- protein
- Length
- 4,554 residues
- Chains
- 28
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP-dependent clp protease proteolytic subunit
- EC
- 3.4.21.92
- UniProt
- P0A6G7
- Ligands
- CA
- Pockets
- 20 · best druggability 0.87
Structure
x-ray diffraction · 10 distinct chains · 47% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, E, G, L, M, N, Q, R, S, U, 2 | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 162 | 46% helix, 22% strand | P0A6G7 |
| D | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 165 | 47% helix, 21% strand | P0A6G7 |
| F | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 166 | 49% helix, 20% strand | P0A6G7 |
| H | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 164 | 48% helix, 22% strand | P0A6G7 |
| I, J, P | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 163 | 46% helix, 21% strand | P0A6G7 |
| K, T, W | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 161 | 46% helix, 19% strand | P0A6G7 |
| O | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 166 | 48% helix, 20% strand | P0A6G7 |
| V, Y, 1 | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 163 | 48% helix, 21% strand | P0A6G7 |
| X | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 161 | 47% helix, 22% strand | P0A6G7 |
| Z | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 165 | 46% helix, 21% strand | P0A6G7 |
Ligands and binding sites
- CA · Calcium ion · metal · 13 copies · chains E, F, I, Z, O, J, K, M, T, V, 1, 2
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1073 | 0.87 | 0.88 | 121 | CA |
| 2 | 308 | 0.76 | 0.88 | 40 | CA |
| 3 | 130 | 0.69 | 0.89 | 24 | empty |
| 4 | 520 | 0.68 | 0.79 | 68 | empty |
| 5 | 370 | 0.66 | 0.80 | 52 | empty |
Interfaces
60 interfaces between chains.
- F–G · 1373 Ų buried · 13 hydrogen bonds · protein-protein
- 1–2 · 1369 Ų buried · 19 hydrogen bonds · protein-protein
- H–I · 1355 Ų buried · 14 hydrogen bonds · protein-protein
- X–Y · 1318 Ų buried · 14 hydrogen bonds · protein-protein
- O–U · 1292 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 11 disulfide (disulfide).
Compared structures
- 3HLN · Crystal structure of ClpP A153C mutant with inter-heptamer disulfide bonds · the same entry in another collection · chain K against K, TM-score 1.00
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 P0A6G7
- Elsewhere: RCSB PDB 3HLN · PDBe 3HLN · UniProt P0A6G7
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.