Research workbench
Structural investigation of the glms ribozyme bound to its catalytic cofactor
Analyse Structural investigation of the glms ribozyme bound to its catalytic cofactor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2NZ4
- Type
- protein + RNA
- Length
- 980 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P09012
Structure
x-ray diffraction · 5 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E, F, G, H | — | rna | 13 | — | — |
| P, Q, R, S | — | rna | 141 | — | — |
| A, D | — | protein | 90 | — | P09012 |
| B | — | protein | 94 | — | P09012 |
| C | — | protein | 90 | — | P09012 |
Compared structures
- 2NZ4 · Structural investigation of the GlmS ribozyme bound to its catalytic cofactor · the same entry in another collection · chain F against F, TM-score 1.00
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 P09012
- Elsewhere: RCSB PDB 2NZ4 · PDBe 2NZ4 · UniProt P09012
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