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Structure of the N-terminal catalytic region of T. thermophilus rel
Analyse Structure of the N-terminal catalytic region of T. thermophilus rel in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6S2V
- Type
- protein
- Length
- 1,004 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- F6DES6
- Ligands
- MN, NA, CL, PO4
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 342 | — | F6DES6 |
| B | — | protein | 326 | — | F6DES6 |
| C | — | protein | 336 | — | F6DES6 |
Ligands and binding sites
- MN · Manganese (II) ion · metal · 3 copies · chains A, B, C
- NA · Sodium ion · metal · chains C
- CL · Chloride ion · ion · 6 copies · chains A, B, C
- PO4 · Phosphate ion · ion · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6S2V · Structure of the N-terminal catalytic region of T. thermophilus Rel · 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 6S2V · PDBe 6S2V · UniProt F6DES6
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