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Crystal structure of bacillus subtilis dltc
Analyse Crystal structure of bacillus subtilis dltc in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4BPG
- Type
- protein
- Length
- 159 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- D-alanine--POLY(PHOSPHORIBITOL) ligase subunit 2
- EC
- 6.1.1.13
- UniProt
- P39579
Structure
x-ray diffraction · 2 distinct chains · 57% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | D-alanine--POLY(PHOSPHORIBITOL) ligase subunit 2 (EC 6.1.1.13) | protein | 80 | 54% helix, 0% strand | P39579 |
| B | D-alanine--POLY(PHOSPHORIBITOL) ligase subunit 2 (EC 6.1.1.13) | protein | 79 | 59% helix, 0% strand | P39579 |
Interfaces
1 interface between chains.
- A–B · 617 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (phosphorylation).
Compared structures
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 P39579
- Elsewhere: RCSB PDB 4BPG · PDBe 4BPG · UniProt P39579
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