MolNFT v1 · #163431 · protein
Structure of the catalytic domain of T. thermophilus rel in complex with AMP and ppgpp
6S2U: “Structure of the catalytic domain of T. thermophilus rel in complex with AMP and ppgpp”. X-ray diffraction, 5 ligands (AMP, GN3, TMO). MolNFT v1 #163431 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6S2U
- Type
- protein
- Length
- 341 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- F6DES6
- Ligands
- AMP, GN3, TMO, MG, MN
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 341 | — | F6DES6 |
Ligands and binding sites
- AMP · Adenosine monophosphate · ligand · chains A
- GN3 · [[[(2~{R},3~{S},4~{R},5~{R})-5-(2-azanyl-6-oxidanylidene-1~{H}-purin-9-yl)-4-oxidanyl-2-[[oxidanyl(phosphonooxy)phosphoryl]oxymethyl]oxolan-3-yl]oxy-oxidanyl-phosphoryl]amino]phosphonic acid · ligand · chains A
- TMO · trimethylamine oxide · ligand
- MG · Magnesium ion · metal · 2 copies · chains A
- MN · Manganese (II) ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6S2U · Structure of the catalytic domain of T. thermophilus Rel in complex with AMP and ppGpp · 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 F6DES6
- Elsewhere: RCSB PDB 6S2U · PDBe 6S2U · UniProt F6DES6
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