MolNFT v1 · #10730 · protein
Acc deaminase mutant complexed with acc
1J0D · 1-aminocyclopropane-1-carboxylate deaminase: “Acc deaminase mutant complexed with acc”. X-ray diffraction, 1 ligand (5PA), 14 pockets (best druggability 0.83). MolNFT v1 #10730 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 1J0D
- 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
- 5PA
- Pockets
- 14 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 16% 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 | 43% helix, 16% strand | Q7M523 |
Ligands and binding sites
- 5PA · N-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-Y-lmethyl]-1-amino-cyclopropanecarboxylic acid · 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 | 701 | 0.83 | 0.87 | 78 | empty |
| 2 | 124 | 0.81 | 0.99 | 30 | 5PA |
| 3 | 125 | 0.80 | 0.98 | 29 | 5PA |
| 4 | 118 | 0.80 | 0.98 | 28 | 5PA |
| 5 | 109 | 0.79 | 0.98 | 27 | 5PA |
Interfaces
5 interfaces between chains.
- A–B · 1999 Ų buried · 28 hydrogen bonds · protein-protein
- C–D · 1946 Ų buried · 23 hydrogen bonds · protein-protein
- B–D · 422 Ų buried · 4 hydrogen bonds · protein-protein
- A–D · 271 Ų buried · 3 hydrogen bonds · protein-protein
- B–C · 230 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 1J0D · PDBe 1J0D · UniProt Q7M523
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