Research workbench
Crystal structure of E.COLI biotin carboxylase in complex with two ADP and two ca ions
Analyse Crystal structure of E.COLI biotin carboxylase in complex with two ADP and two… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3RUP
- Type
- protein
- Length
- 890 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Biotin carboxylase
- EC
- 6.3.4.14, 6.4.1.2
- UniProt
- P24182
- Ligands
- ADP, CA, CL
- Pockets
- 3 · best druggability 0.81
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Biotin carboxylase (EC 6.3.4.14, 6.4.1.2) | protein | 444 | 36% helix, 27% strand | P24182 |
| B | Biotin carboxylase (EC 6.3.4.14, 6.4.1.2) | protein | 446 | 36% helix, 27% strand | P24182 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 4 copies · chains A, B
- CA · Calcium ion · metal · 4 copies · chains A, B
- CL · Chloride ion · ion · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 846 | 0.81 | 0.83 | 86 | ADP, CA |
| 2 | 839 | 0.80 | 0.83 | 78 | ADP, CA, CL |
| 3 | 581 | 0.74 | 0.82 | 59 | empty |
Interfaces
1 interface between chains.
- A–B · 1305 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
- 3RUP · Crystal structure of E.coli biotin carboxylase in complex with two ADP and two Ca ions · the same entry in another collection · chain A against A, TM-score 1.00
- P24182 · AlphaFold monomer V2.0 prediction for biotin carboxylase (P24182) · a predicted model of the same protein · chain B against A, TM-score 0.95
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 P24182
- Elsewhere: RCSB PDB 3RUP · PDBe 3RUP · UniProt P24182
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