Research workbench
RT29 bound to D(CTTAATTCGAATTAAG) in complex with mmlv rt catalytic fragment
Analyse RT29 bound to D(CTTAATTCGAATTAAG) in complex with mmlv rt catalytic fragment in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2FJV
- Type
- protein + DNA
- Length
- 271 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P03355
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | — | dna | 8 | — | — |
| G | — | dna | 8 | — | — |
| A | — | protein | 255 | — | P03355 |
Compared structures
- 2FJV · RT29 Bound to D(CTTAATTCGAATTAAG) in complex with MMLV RT Catalytic Fragment · the same entry in another collection · chain B against B, 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 P03355
- Elsewhere: RCSB PDB 2FJV · PDBe 2FJV · UniProt P03355
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