MolNFT v1 · #151032 · protein
Structure of the repeat unit in the network formed by ccmm and rubisco from synechococcus elongatus
6HBC · Carbon dioxide concentrating mechanism protein ccmm: “Structure of the repeat unit in the network formed by ccmm and rubisco from synechococcus elongatus”. Electron microscopy, 18 pockets (best druggability 0.80). MolNFT v1 #151032…
- PDB
- 6HBC
- Type
- protein
- Length
- 1,178 residues
- Chains
- 5
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carbon dioxide concentrating mechanism protein ccmm; Ribulose bisphosphate carboxylase…
- EC
- 4.1.1.39
- UniProt
- Q03513, Q31NB3, Q31NB2
- Pockets
- 18 · best druggability 0.80
Structure
electron microscopy · 3 distinct chains · 40% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Carbon dioxide concentrating mechanism protein ccmm | protein | 86 | 36% helix, 30% strand | Q03513 |
| B, C | Ribulose bisphosphate carboxylase large chain (EC 4.1.1.39) | protein | 440 | 44% helix, 18% strand | Q31NB3 |
| D, E | Ribulose 1,5-bisphosphate carboxylase small subunit (EC 4.1.1.39) | protein | 106 | 25% helix, 26% strand | Q31NB2 |
Pockets
18 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1024 | 0.80 | 0.82 | 90 | empty |
| 2 | 711 | 0.73 | 0.79 | 82 | empty |
| 3 | 363 | 0.62 | 0.78 | 61 | empty |
| 4 | 143 | 0.61 | 0.85 | 32 | empty |
| 5 | 124 | 0.59 | 0.85 | 22 | empty |
Interfaces
8 interfaces between chains.
- B–D · 1645 Ų buried · 21 hydrogen bonds · protein-protein
- C–E · 1642 Ų buried · 19 hydrogen bonds · protein-protein
- A–C · 569 Ų buried · 6 hydrogen bonds · protein-protein
- B–C · 497 Ų buried · 7 hydrogen bonds · protein-protein
- C–D · 390 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 6HBC · Structure of the repeat unit in the network formed by CcmM and Rubisco from Synechococcus… · the same entry in another collection · chain E against E, TM-score 1.00
- Q31NB3 · AlphaFold monomer V2.0 prediction for ribulose bisphosphate carboxylase large chain… · a predicted model of the same protein · chain B against A, TM-score 0.99
- Q03513 · AlphaFold monomer V2.0 prediction for carboxysome assembly protein ccmm (Q03513) · a predicted model of the same protein · chain A against A, TM-score 0.98
- Q31NB2 · AlphaFold monomer V2.0 prediction for ribulose bisphosphate carboxylase small subunit… · a predicted model of the same protein · chain D against A, TM-score 0.97
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 Q03513
- Every structure of UniProt Q31NB3
- Every structure of UniProt Q31NB2
- Elsewhere: RCSB PDB 6HBC · PDBe 6HBC · UniProt Q03513 · UniProt Q31NB3 · UniProt Q31NB2
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.