Research workbench
Crystal strucrture of biotin protein ligase from S. aureus
Analyse Crystal strucrture of biotin protein ligase from S. aureus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3RIR
- Type
- protein
- Length
- 322 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Biotin-[acetyl-CoA-carboxylase] ligase
- EC
- 6.3.4.15
- UniProt
- E5R5T0
- Ligands
- BT5
- Pockets
- 3 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Biotin-[acetyl-CoA-carboxylase] ligase (EC 6.3.4.15) | protein | 322 | 34% helix, 31% strand | E5R5T0 |
Ligands and binding sites
- BT5 · Biotinyl-5-amp · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 322 | 0.69 | 0.83 | 49 | BT5 |
| 2 | 110 | 0.42 | 0.76 | 22 | empty |
| 3 | 61 | 0.31 | 0.75 | 14 | empty |
Compared structures
- 3RIR · Crystal Strucrture of Biotin Protein Ligase from S. aureus · 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 E5R5T0
- Elsewhere: RCSB PDB 3RIR · PDBe 3RIR · UniProt E5R5T0
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