Research workbench
Surface residue engineering of bovine carbonic anhydrase to an extreme halophilic enzyme for potential application in postcombustion CO2 capture
Analyse Surface residue engineering of bovine carbonic anhydrase to an extreme… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4CNR
- Type
- protein
- Length
- 1,030 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P00921
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | — | protein | 257 | — | P00921 |
| B, D | — | protein | 258 | — | P00921 |
Compared structures
- 4CNR · Surface residue engineering of bovine carbonic anhydrase to an extreme halophilic enzyme… · the same entry in another collection · chain D against D, TM-score 1.00
- P00921 · AlphaFold monomer V2.0 prediction for carbonic anhydrase 2 (P00921) · a predicted model of the same protein · chain D against A, TM-score 0.99
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 P00921
- Elsewhere: RCSB PDB 4CNR · PDBe 4CNR · UniProt P00921
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.