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Crystal structure of biotin protein ligase from pyrococcus horikoshii OT3 in complex with ATP
Analyse Crystal structure of biotin protein ligase from pyrococcus horikoshii OT3 in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1X01
- Type
- protein
- Length
- 470 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Biotin--[acetyl-CoA-carboxylase] ligase
- EC
- 6.3.4.15
- UniProt
- O57883
- Ligands
- ATP, PO4
- Pockets
- 4 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 26% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Biotin--[acetyl-CoA-carboxylase] ligase (EC 6.3.4.15) | protein | 235 | 26% helix, 31% strand | O57883 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · 2 copies · chains A, B
- PO4 · Phosphate ion · ion
- ACY · Acetic acid · additive · 3 copies · 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 | 274 | 0.66 | 0.82 | 50 | ATP |
| 2 | 256 | 0.62 | 0.81 | 49 | ATP |
| 3 | 104 | 0.43 | 0.77 | 19 | empty |
| 4 | 102 | 0.40 | 0.76 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 1063 Ų buried · 25 hydrogen bonds · protein-protein
Compared structures
- 1X01 · Crystal Structure Of Biotin Protein Ligase From Pyrococcus Horikoshii Ot3 in complex with… · 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 1X01 · PDBe 1X01 · UniProt O57883
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