Research workbench
Inactive truncation of the beta-carboxysomal gamma-carbonic anhydrase, ccmm, form 1
Analyse Inactive truncation of the beta-carboxysomal gamma-carbonic anhydrase, ccmm… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3KWD
- Type
- protein
- Length
- 166 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carbon dioxide concentrating mechanism protein
- EC
- 4.2.1.1
- UniProt
- Q8DKB5
- Ligands
- ZN, CL
Structure
x-ray diffraction · 1 distinct chain · 8% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Carbon dioxide concentrating mechanism protein (EC 4.2.1.1) | protein | 166 | 8% helix, 39% strand | Q8DKB5 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 3KWD · Inactive truncation of the beta-carboxysomal gamma-Carbonic Anhydrase, CcmM, form 1 · the same entry in another collection · chain A against A, TM-score 1.00
- Q8DKB5 · AlphaFold monomer V2.0 prediction for carboxysome assembly protein ccmm (Q8DKB5) · a predicted model of the same protein · chain A 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 Q8DKB5
- Elsewhere: RCSB PDB 3KWD · PDBe 3KWD · UniProt Q8DKB5
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.