Research workbench
Crystal structure analysis of bacillus subtilis 168 xepa
Analyse Crystal structure analysis of bacillus subtilis 168 xepa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6IA5
- Type
- protein
- Length
- 1,389 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P39797
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| D, B | — | protein | 277 | — | P39797 |
| A, C | — | protein | 278 | — | P39797 |
| E | — | protein | 279 | — | P39797 |
Ligands and binding sites
- ACT · Acetate ion · additive · 22 copies · chains D, E, B, A, C
- GOL · Glycerol · additive · 11 copies · chains D, E, A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6IA5 · Crystal Structure Analysis of Bacillus subtilis 168 XepA · the same entry in another collection · chain E against E, TM-score 1.00
- P39797 · AlphaFold monomer V2.0 prediction for phage-like element pbsx protein xepa (P39797) · a predicted model of the same protein · chain D against A, TM-score 0.41
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 P39797
- Elsewhere: RCSB PDB 6IA5 · PDBe 6IA5 · UniProt P39797
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