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Crystal structure of mouse csad
Analyse Crystal structure of mouse csad in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6ZEK
- Type
- protein
- Length
- 1,898 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
- CO, CL, SO4
- Pockets
- 20 · best druggability 0.80
Structure
x-ray diffraction · 4 distinct chains · 49% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cysteine sulfinic acid decarboxylase (EC 4.1.1.29, 4.1.1.11) | protein | 476 | 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 | 49% helix, 14% strand | Q9DBE0 |
| D | Cysteine sulfinic acid decarboxylase (EC 4.1.1.29, 4.1.1.11) | protein | 474 | 49% helix, 14% strand | Q9DBE0 |
Ligands and binding sites
- CO · Cobalt (II) ion · metal · 4 copies · chains A, B, C, D
- CL · Chloride ion · ion · 13 copies · chains A, C, B, D
- SO4 · Sulfate ion · ion · chains A
- GOL · Glycerol · additive · 4 copies · chains B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 630 | 0.80 | 0.85 | 51 | CL |
| 2 | 459 | 0.75 | 0.84 | 49 | empty |
| 3 | 685 | 0.75 | 0.81 | 63 | CL |
| 4 | 326 | 0.74 | 0.86 | 41 | CL |
| 5 | 679 | 0.74 | 0.80 | 68 | CL |
Interfaces
5 interfaces between chains.
- A–C · 6634 Ų buried · 81 hydrogen bonds · protein-protein
- B–D · 6299 Ų buried · 73 hydrogen bonds · protein-protein
- B–C · 270 Ų buried · 2 hydrogen bonds · protein-protein
- C–D · 158 Ų buried · 5 hydrogen bonds · protein-protein
- A–B · 92 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (cofactor).
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 6ZEK · PDBe 6ZEK · UniProt Q9DBE0
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