Research workbench
A closer look at the active site of gamma-carbonic anhydrases: high resolution crystallographic studies of the carbonic anhydrase from methanosarcina thermophila
Analyse A closer look at the active site of gamma-carbonic anhydrases: high resolution… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1QRL
- Type
- protein
- Length
- 214 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carbonic anhydrase
- UniProt
- P40881
- Ligands
- BCT, ZN
Structure
x-ray diffraction · 1 distinct chain · 12% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Carbonic anhydrase | protein | 214 | 12% helix, 34% strand | P40881 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1QRL · A closer look at the active site of gamma-carbonic anhydrases: high resolution… · the same entry in another collection · chain A against A, TM-score 1.00
- P40881 · AlphaFold monomer V2.0 prediction for carbonic anhydrase (P40881) · a predicted model of the same protein · chain A 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 P40881
- Elsewhere: RCSB PDB 1QRL · PDBe 1QRL · UniProt P40881
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