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Crystal structure of the small subunit-like domain 1 of ccmm from synechococcus elongatus (strain pcc 7942), thiol-oxidized form
Analyse Crystal structure of the small subunit-like domain 1 of ccmm from synechococcus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6HBA
- Type
- protein
- Length
- 176 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carbon dioxide concentrating mechanism protein ccmm
- UniProt
- Q03513
- Pockets
- 3 · best druggability 0.40
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Carbon dioxide concentrating mechanism protein ccmm | protein | 89 | 35% helix, 27% strand | Q03513 |
| B | Carbon dioxide concentrating mechanism protein ccmm | protein | 87 | 36% helix, 28% strand | Q03513 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 103 | 0.40 | 0.77 | 20 | empty |
| 2 | 107 | 0.40 | 0.76 | 18 | empty |
| 3 | 63 | 0.29 | 0.74 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 533 Ų buried · 22 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 6HBA · Crystal Structure of the small subunit-like domain 1 of CcmM from Synechococcus elongatus… · the same entry in another collection · chain A against A, TM-score 1.00
- Q03513 · AlphaFold monomer V2.0 prediction for carboxysome assembly protein ccmm (Q03513) · a predicted model of the same protein · chain B against A, TM-score 0.96
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
- Elsewhere: RCSB PDB 6HBA · PDBe 6HBA · UniProt Q03513
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