MolNFT v1 · #171051 · protein
Structure of the chlamydomonas reinhardtii sas-6 coiled-coil domain, C2 crystal form
6YRL · Centriole protein: “Structure of the chlamydomonas reinhardtii sas-6 coiled-coil domain, C2 crystal form”. X-ray diffraction, 6 pockets (best druggability 0.45). MolNFT v1 #171051 on GenesisL1: 3D structure, binding sites and…
- PDB
- 6YRL
- Type
- protein
- Length
- 432 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Centriole protein
- UniProt
- A9CQL4
- Pockets
- 6 · best druggability 0.45
Structure
x-ray diffraction · 4 distinct chains · 98% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Centriole protein | protein | 108 | 98% helix, 0% strand | A9CQL4 |
| B | Centriole protein | protein | 108 | 97% helix, 0% strand | A9CQL4 |
| C | Centriole protein | protein | 105 | 97% helix, 0% strand | A9CQL4 |
| D | Centriole protein | protein | 111 | 98% helix, 0% strand | A9CQL4 |
Pockets
6 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 205 | 0.45 | 0.73 | 30 | empty |
| 2 | 138 | 0.40 | 0.73 | 17 | empty |
| 3 | 167 | 0.40 | 0.72 | 18 | empty |
| 4 | 102 | 0.36 | 0.74 | 16 | empty |
| 5 | 115 | 0.34 | 0.72 | 18 | empty |
Interfaces
6 interfaces between chains.
- A–D · 2821 Ų buried · 17 hydrogen bonds · protein-protein
- B–C · 2625 Ų buried · 15 hydrogen bonds · protein-protein
- A–C · 1078 Ų buried · 20 hydrogen bonds · protein-protein
- B–D · 369 Ų buried · 3 hydrogen bonds · protein-protein
- A–B · 101 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 4 modified, 2 disulfide (engineered, disulfide).
Compared structures
- 6YRL · Structure of the Chlamydomonas reinhardtii SAS-6 coiled-coil domain, C2 crystal form · 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 A9CQL4
- Elsewhere: RCSB PDB 6YRL · PDBe 6YRL · UniProt A9CQL4
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