MolNFT v1 · #10729 · protein
Acc deaminase mutated to catalytic residue
1J0C · 1-aminocyclopropane-1-carboxylate deaminase: “Acc deaminase mutated to catalytic residue”. X-ray diffraction, 1 ligand (PLP), 14 pockets (best druggability 0.80). MolNFT v1 #10729 on GenesisL1: 3D structure, binding sites and…
- PDB
- 1J0C
- Type
- protein
- Length
- 1,364 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 1-aminocyclopropane-1-carboxylate deaminase
- EC
- 4.1.99.4
- UniProt
- Q7M523
- Ligands
- PLP
- Pockets
- 14 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | 1-aminocyclopropane-1-carboxylate deaminase (EC 4.1.99.4) | protein | 341 | 42% helix, 15% strand | Q7M523 |
Ligands and binding sites
- PLP · Pyridoxal-5'-phosphate · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 114 | 0.80 | 0.99 | 29 | PLP |
| 2 | 509 | 0.79 | 0.87 | 57 | empty |
| 3 | 122 | 0.79 | 0.98 | 30 | PLP |
| 4 | 112 | 0.79 | 0.98 | 29 | PLP |
| 5 | 105 | 0.78 | 0.98 | 26 | PLP |
Interfaces
5 interfaces between chains.
- C–D · 1948 Ų buried · 21 hydrogen bonds · protein-protein
- A–B · 1943 Ų buried · 31 hydrogen bonds · protein-protein
- B–D · 422 Ų buried · 3 hydrogen bonds · protein-protein
- B–C · 253 Ų buried · 5 hydrogen bonds · protein-protein
- A–D · 246 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
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 Q7M523
- Elsewhere: RCSB PDB 1J0C · PDBe 1J0C · UniProt Q7M523
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