Research workbench
Cell division protein sepf in complex with C-terminal domain of ftsz
Analyse Cell division protein sepf in complex with C-terminal domain of ftsz in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6SCS
- Type
- protein
- Length
- 311 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cell division protein sepf; Cell division protein ftsz
- UniProt
- Q8NNN6
- Ligands
- MG
Structure
x-ray diffraction · 7 distinct chains · 41% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cell division protein sepf | protein | 70 | 43% helix, 27% strand | Q8NNN6 |
| B | Cell division protein sepf | protein | 67 | 45% helix, 27% strand | Q8NNN6 |
| D | Cell division protein sepf | protein | 74 | 39% helix, 26% strand | Q8NNN6 |
| E | Cell division protein sepf | protein | 66 | 44% helix, 23% strand | Q8NNN6 |
| P | Cell division protein ftsz | protein | 10 | 30% helix, 0% strand | — |
| Q, R | Cell division protein ftsz | protein | 8 | 0% helix, 0% strand | — |
| S | Cell division protein ftsz | protein | 8 | 38% helix, 0% strand | — |
Ligands and binding sites
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
13 interfaces between chains.
- A–B · 852 Ų buried · 12 hydrogen bonds · protein-protein
- D–E · 812 Ų buried · 11 hydrogen bonds · protein-protein
- A–D · 601 Ų buried · 8 hydrogen bonds · protein-protein
- B–P · 470 Ų buried · 4 hydrogen bonds · protein-protein
- D–R · 443 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 6SCS · Cell Division Protein SepF in complex with C-terminal domain of FtsZ · the same entry in another collection · chain S against S, 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 Q8NNN6
- Elsewhere: RCSB PDB 6SCS · PDBe 6SCS · UniProt Q8NNN6
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