Research workbench
Crystal structure of biotin protein ligase from pyrococcus horikoshii OT3, K111A mutation
Analyse Crystal structure of biotin protein ligase from pyrococcus horikoshii OT3… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2HNI
- Type
- protein
- Length
- 465 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 235AA long hypothetical biotin-[acetyl-CoA-carboxylase] ligase
- EC
- 6.3.4.15
- UniProt
- O57883
- Pockets
- 4 · best druggability 0.65
Structure
x-ray diffraction · 2 distinct chains · 26% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 235AA long hypothetical biotin-[acetyl-CoA-carboxylase] ligase (EC 6.3.4.15) | protein | 230 | 26% helix, 31% strand | O57883 |
| B | 235AA long hypothetical biotin-[acetyl-CoA-carboxylase] ligase (EC 6.3.4.15) | protein | 235 | 26% helix, 30% strand | O57883 |
Ligands and binding sites
- ACY · Acetic acid · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 309 | 0.65 | 0.81 | 50 | empty |
| 2 | 257 | 0.54 | 0.77 | 41 | empty |
| 3 | 164 | 0.49 | 0.77 | 24 | empty |
| 4 | 101 | 0.43 | 0.77 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 1054 Ų buried · 28 hydrogen bonds · protein-protein
Compared structures
- 2HNI · Crystal Structure Of Biotin Protein Ligase From Pyrococcus Horikoshii OT3, K111A mutation · 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 O57883
- Elsewhere: RCSB PDB 2HNI · PDBe 2HNI · UniProt O57883
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