Research workbench
C54S mutant of choline-sulfatase from E. meliloti CECT4857 bound to hepes
Analyse C54S mutant of choline-sulfatase from E. meliloti CECT4857 bound to hepes in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7PTJ
- Type
- protein
- Length
- 2,045 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A410NSD4
- Ligands
- CA, SO4
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 513 | — | A0A410NSD4 |
| B | — | protein | 512 | — | A0A410NSD4 |
| C | — | protein | 511 | — | A0A410NSD4 |
| D | — | protein | 509 | — | A0A410NSD4 |
Ligands and binding sites
- CA · Calcium ion · metal · 4 copies · chains A, B, C, D
- SO4 · Sulfate ion · ion · 13 copies · chains A, B, C, D
- GOL · Glycerol · additive · 17 copies · chains A, B, C
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · 5 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7PTJ · C54S mutant of choline-sulfatase from E. meliloti CECT4857 bound to HEPES · 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 A0A410NSD4
- Elsewhere: RCSB PDB 7PTJ · PDBe 7PTJ · UniProt A0A410NSD4
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