MolNFT v1 · #136178 · protein
Dhp domain of phor of M. tuberculosis - native data
5UKY · ATP-binding protein: “Dhp domain of phor of M. tuberculosis - native data”. X-ray diffraction, 1 ligand (K). MolNFT v1 #136178 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5UKY
- Type
- protein
- Length
- 148 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP-binding protein
- EC
- 2.7.13.3
- UniProt
- P71815
- Ligands
- K
Structure
x-ray diffraction · 1 distinct chain · 86% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | ATP-binding protein (EC 2.7.13.3) | protein | 74 | 86% helix, 0% strand | P71815 |
Ligands and binding sites
- K · Potassium ion · metal · chains A, B
- EDO · 1,2-ethanediol · additive · 3 copies · chains A, B
- PG4 · Tetraethylene glycol · additive · chains A, B
- PGE · Triethylene glycol · additive · chains A, B
- PEG · Di(hydroxyethyl)ether · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 1825 Ų buried · 20 hydrogen bonds · protein-protein
Compared structures
- 5UKY · DHp domain of PhoR of M. tuberculosis - native data · 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 P71815
- Elsewhere: RCSB PDB 5UKY · PDBe 5UKY · UniProt P71815
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