MolNFT v1 · #73183 · protein
A domain insertion in E. COLI gyrb adopts a novel fold that plays a critical role in gyrase function
3NUH: “A domain insertion in E. COLI gyrb adopts a novel fold that plays a critical role in gyrase function”. X-ray diffraction. MolNFT v1 #73183 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3NUH
- Type
- protein
- Length
- 839 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0AES4, P0AES6
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 485 | — | P0AES4 |
| B | — | protein | 354 | — | P0AES6 |
Compared structures
- 3NUH · A domain insertion in E. coli GyrB adopts a novel fold that plays a critical role in… · the same entry in another collection · chain A against A, TM-score 1.00
- P0AES4 · AlphaFold monomer V2.0 prediction for DNA gyrase subunit a (P0AES4) · a predicted model of the same protein · chain A against A, TM-score 0.94
- P0AES6 · AlphaFold monomer V2.0 prediction for DNA gyrase subunit B (P0AES6) · a predicted model of the same protein · chain B against A, TM-score 0.79
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 P0AES4
- Every structure of UniProt P0AES6
- Elsewhere: RCSB PDB 3NUH · PDBe 3NUH · UniProt P0AES4 · UniProt P0AES6
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