MolNFT v1 · #172366 · protein
Crystal structure of mouse csad in apo form
7A0A · Cysteine sulfinic acid decarboxylase: “Crystal structure of mouse csad in apo form”. X-ray diffraction, 2 ligands (NA, SO4), 18 pockets (best druggability 0.79). MolNFT v1 #172366 on GenesisL1: 3D structure, binding sites and…
- PDB
- 7A0A
- Type
- protein
- Length
- 1,895 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cysteine sulfinic acid decarboxylase
- EC
- 4.1.1.29, 4.1.1.11
- UniProt
- Q9DBE0
- Ligands
- NA, SO4
- Pockets
- 18 · best druggability 0.79
Structure
x-ray diffraction · 4 distinct chains · 49% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cysteine sulfinic acid decarboxylase (EC 4.1.1.29, 4.1.1.11) | protein | 474 | 49% helix, 13% strand | Q9DBE0 |
| B | Cysteine sulfinic acid decarboxylase (EC 4.1.1.29, 4.1.1.11) | protein | 470 | 49% helix, 13% strand | Q9DBE0 |
| C | Cysteine sulfinic acid decarboxylase (EC 4.1.1.29, 4.1.1.11) | protein | 478 | 48% helix, 14% strand | Q9DBE0 |
| D | Cysteine sulfinic acid decarboxylase (EC 4.1.1.29, 4.1.1.11) | protein | 473 | 48% helix, 14% strand | Q9DBE0 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
18 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 771 | 0.79 | 0.83 | 73 | empty |
| 2 | 841 | 0.79 | 0.82 | 78 | empty |
| 3 | 738 | 0.78 | 0.82 | 63 | SO4 |
| 4 | 703 | 0.75 | 0.81 | 69 | empty |
| 5 | 400 | 0.73 | 0.84 | 48 | empty |
Interfaces
5 interfaces between chains.
- A–C · 6517 Ų buried · 70 hydrogen bonds · protein-protein
- B–D · 6250 Ų buried · 72 hydrogen bonds · protein-protein
- B–C · 264 Ų buried · 0 hydrogen bonds · protein-protein
- C–D · 168 Ų buried · 3 hydrogen bonds · protein-protein
- A–B · 89 Ų buried · 0 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 Q9DBE0
- Elsewhere: RCSB PDB 7A0A · PDBe 7A0A · UniProt Q9DBE0
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