MolNFT v1 · #107187 · protein
N-terminal domain of C. rheinhardtii sas-6 homolog BLD12P Q93E G94D K146R Q147R (NN23)
4U2I · Centriole protein: “N-terminal domain of C. rheinhardtii sas-6 homolog BLD12P Q93E G94D K146R Q147R (NN23)”. X-ray diffraction, 4 pockets (best druggability 0.48). MolNFT v1 #107187 on GenesisL1: 3D structure, binding sites and…
- PDB
- 4U2I
- Type
- protein
- Length
- 554 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Centriole protein
- UniProt
- A9CQL4
- Pockets
- 4 · best druggability 0.48
Structure
x-ray diffraction · 4 distinct chains · 18% helix, 57% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Centriole protein | protein | 139 | 19% helix, 56% strand | A9CQL4 |
| C | Centriole protein | protein | 138 | 17% helix, 57% strand | A9CQL4 |
| B | Centriole protein | protein | 140 | 17% helix, 59% strand | A9CQL4 |
| D | Centriole protein | protein | 137 | 18% helix, 57% strand | A9CQL4 |
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 218 | 0.48 | 0.75 | 36 | empty |
| 2 | 178 | 0.47 | 0.75 | 22 | empty |
| 3 | 90 | 0.38 | 0.77 | 18 | empty |
| 4 | 65 | 0.28 | 0.73 | 13 | empty |
Interfaces
4 interfaces between chains.
- C–D · 970 Ų buried · 17 hydrogen bonds · protein-protein
- A–B · 904 Ų buried · 15 hydrogen bonds · protein-protein
- A–C · 461 Ų buried · 14 hydrogen bonds · protein-protein
- B–D · 208 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 4U2I · N-terminal domain of C. Rheinhardtii SAS-6 homolog bld12p Q93E G94D K146R Q147R (NN23) · 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 4U2I · PDBe 4U2I · UniProt A9CQL4
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