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Structure of the chlamydomonas reinhardtii sas-6 coiled-coil domain, P2 crystal form
Analyse Structure of the chlamydomonas reinhardtii sas-6 coiled-coil domain, P2 crystal… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6YRN
- Type
- protein
- Length
- 831 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Centriole protein
- UniProt
- A9CQL4
- Pockets
- 15 · best druggability 0.67
Structure
x-ray diffraction · 8 distinct chains · 97% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Centriole protein | protein | 107 | 98% helix, 0% strand | A9CQL4 |
| B | Centriole protein | protein | 101 | 97% helix, 0% strand | A9CQL4 |
| C | Centriole protein | protein | 101 | 98% helix, 0% strand | A9CQL4 |
| D | Centriole protein | protein | 111 | 98% helix, 0% strand | A9CQL4 |
| E | Centriole protein | protein | 107 | 98% helix, 0% strand | A9CQL4 |
| F | Centriole protein | protein | 106 | 97% helix, 0% strand | A9CQL4 |
| G | Centriole protein | protein | 93 | 94% helix, 0% strand | A9CQL4 |
| H | Centriole protein | protein | 105 | 98% helix, 0% strand | A9CQL4 |
Ligands and binding sites
- PG4 · Tetraethylene glycol · additive · chains B, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 436 | 0.67 | 0.79 | 50 | empty |
| 2 | 585 | 0.64 | 0.75 | 54 | PG4 |
| 3 | 445 | 0.57 | 0.74 | 44 | empty |
| 4 | 307 | 0.50 | 0.73 | 30 | empty |
| 5 | 115 | 0.47 | 0.79 | 22 | empty |
Interfaces
16 interfaces between chains.
- A–D · 2911 Ų buried · 24 hydrogen bonds · protein-protein
- B–C · 2811 Ų buried · 23 hydrogen bonds · protein-protein
- E–F · 2786 Ų buried · 22 hydrogen bonds · protein-protein
- G–H · 2470 Ų buried · 15 hydrogen bonds · protein-protein
- A–E · 1070 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 6YRN · Structure of the Chlamydomonas reinhardtii SAS-6 coiled-coil domain, P2 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 6YRN · PDBe 6YRN · UniProt A9CQL4
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