Research workbench
Crystal structure of the biotin carboxylase subunit of pyruvate carboxylase
Analyse Crystal structure of the biotin carboxylase subunit of pyruvate carboxylase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ULZ
- Type
- protein
- Length
- 451 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pyruvate carboxylase N-terminal domain
- EC
- 6.4.1.1
- UniProt
- O67483
- Pockets
- 4 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pyruvate carboxylase N-terminal domain (EC 6.4.1.1) | protein | 451 | 36% helix, 24% strand | O67483 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 389 | 0.62 | 0.77 | 61 | empty |
| 2 | 66 | 0.41 | 0.81 | 18 | empty |
| 3 | 60 | 0.28 | 0.74 | 16 | empty |
| 4 | 61 | 0.25 | 0.72 | 15 | empty |
Compared structures
- 1ULZ · Crystal structure of the biotin carboxylase subunit of pyruvate carboxylase · 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 O67483
- Elsewhere: RCSB PDB 1ULZ · PDBe 1ULZ · UniProt O67483
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