MolNFT v1 · #139712 · protein
Crystallographic structure of the enzymatically active N-terminal domain of the rel protein from mycobacterium tuberculosis
5XNX: “Crystallographic structure of the enzymatically active N-terminal domain of the rel protein from…”. X-ray diffraction, 1 ligand (MG). MolNFT v1 #139712 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5XNX
- Type
- protein
- Length
- 1,276 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P9WHG9
- Ligands
- MG
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 323 | — | P9WHG9 |
| B | — | protein | 316 | — | P9WHG9 |
| C | — | protein | 316 | — | P9WHG9 |
| D | — | protein | 321 | — | P9WHG9 |
Ligands and binding sites
- MG · Magnesium ion · metal · 3 copies · chains A, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5XNX · Crystallographic structure of the enzymatically active N-terminal domain of the Rel… · the same entry in another collection · chain D against D, TM-score 1.00
- P9WHG9 · AlphaFold monomer V2.0 prediction for bifunctional (P)PPGPP SYNTHASE/HYDROLASE rela… · a predicted model of the same protein · chain C against A, TM-score 0.92
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 P9WHG9
- Elsewhere: RCSB PDB 5XNX · PDBe 5XNX · UniProt P9WHG9
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