Research workbench
Crystal structure of the carbonic anhydrase-like domain of ccmm in complex with the C-terminal 17 residues of ccaa from synechococcus elongatus (strain pcc 7942)
Analyse Crystal structure of the carbonic anhydrase-like domain of ccmm in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7O54
- Type
- protein
- Length
- 180 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carboxysome assembly protein ccmm; Carbonic anhydrase
- EC
- 4.2.1.1
- UniProt
- Q03513, P27134
- Ligands
- NI, CL
- Pockets
- 1 · best druggability 0.41
Structure
x-ray diffraction · 2 distinct chains · 13% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Carboxysome assembly protein ccmm | protein | 165 | 9% helix, 39% strand | Q03513 |
| B | Carbonic anhydrase (EC 4.2.1.1) | protein | 15 | 53% helix, 0% strand | P27134 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 60 | 0.41 | 0.81 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 564 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
- 7O54 · Crystal structure of the carbonic anhydrase-like domain of CcmM in complex with the… · 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 A against A, TM-score 1.00
- P27134 · AlphaFold monomer V2.0 prediction for carbonic anhydrase (P27134) · a predicted model of the same protein · chain B against A, TM-score 0.47
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 P27134
- Elsewhere: RCSB PDB 7O54 · PDBe 7O54 · UniProt Q03513 · UniProt P27134
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