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Crystal structures of the N-terminal fragment from moloney murine leukemia virus reverse transcriptase complexed with nucleic acid: functional implications for template-primer binding to the fingers domain
Analyse Crystal structures of the N-terminal fragment from moloney murine leukemia… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1D0E
- Type
- protein + DNA
- Length
- 538 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 5'-D(*TP*TP*TP*CP*AP*TP*GP*CP*AP*TP*G)-3'; Reverse transcriptase
- EC
- 2.7.7.49
- UniProt
- P03355
- Pockets
- 8 · best druggability 0.74
Structure
x-ray diffraction · 3 distinct chains · 30% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E, F | 5'-D(*TP*TP*TP*CP*AP*TP*GP*CP*AP*TP*G)-3' | dna | 11 | — | — |
| A | Reverse transcriptase (EC 2.7.7.49) | protein | 259 | 31% helix, 22% strand | P03355 |
| B | Reverse transcriptase (EC 2.7.7.49) | protein | 257 | 28% helix, 20% strand | P03355 |
Pockets
8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 481 | 0.74 | 0.83 | 64 | empty |
| 2 | 194 | 0.55 | 0.78 | 26 | empty |
| 3 | 220 | 0.54 | 0.77 | 25 | empty |
| 4 | 52 | 0.51 | 0.88 | 14 | empty |
| 5 | 128 | 0.48 | 0.79 | 29 | empty |
Interfaces
4 interfaces between chains.
- A–B · 747 Ų buried · 4 hydrogen bonds · protein-protein
- E–A · 428 Ų buried · 7 hydrogen bonds · protein-nucleic
- E–F · 386 Ų buried · 42 hydrogen bonds · nucleic-nucleic
- F–A · 218 Ų buried · 2 hydrogen bonds · protein-nucleic
Compared structures
- 1D0E · Crystal structures of the N-terminal fragment from moloney murine leukemia virus reverse… · the same entry in another collection · chain E against E, 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 1D0E · PDBe 1D0E · UniProt P03355
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