MolNFT v1 · #23745 · protein
Structural basis for a nusa- protein N interaction
1U9L · Transcription elongation protein nusa: “Structural basis for a nusa- protein N interaction”. X-ray diffraction, 1 ligand (AU). MolNFT v1 #23745 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1U9L
- Type
- protein
- Length
- 145 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcription elongation protein nusa; Lambda N
- UniProt
- P03003
- Ligands
- AU
Structure
x-ray diffraction · 3 distinct chains · 68% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transcription elongation protein nusa | protein | 68 | 69% helix, 0% strand | P03003 |
| B | Transcription elongation protein nusa | protein | 70 | 73% helix, 1% strand | — |
| C | Lambda N | protein | 7 | 0% helix, 14% strand | — |
Ligands and binding sites
- AU · Gold ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
3 interfaces between chains.
- B–C · 437 Ų buried · 8 hydrogen bonds · protein-protein
- A–C · 364 Ų buried · 5 hydrogen bonds · protein-protein
- A–B · 312 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 1U9L · Structural basis for a NusA- protein N interaction · the same entry in another collection · chain A against A, 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 P03003
- Elsewhere: RCSB PDB 1U9L · PDBe 1U9L · UniProt P03003
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