MolNFT v1 · #147064 · protein
Crystal structure of chlamydomonas reinhardtii HAP2 ectodomain provides structural insights of functional loops in green algae.
6E18 · Hapless 2: “Crystal structure of chlamydomonas reinhardtii HAP2 ectodomain provides structural insights of functional…”. X-ray diffraction, 3 ligands (NAG, MAN, FUC), 6 pockets (best druggability 0.69). MolNFT v1 #147064 on…
- PDB
- 6E18
- Type
- protein
- Length
- 529 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hapless 2
- UniProt
- A4GRC6
- Ligands
- NAG, MAN, FUC
- Pockets
- 6 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 9% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hapless 2 | protein | 529 | 9% helix, 39% strand | A4GRC6 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 6 copies · chains A
- MAN · alpha-D-mannopyranose · sugar
- FUC · alpha-L-fucopyranose · sugar · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 298 | 0.69 | 0.83 | 29 | empty |
| 2 | 264 | 0.59 | 0.79 | 31 | GOL |
| 3 | 159 | 0.48 | 0.77 | 22 | empty |
| 4 | 122 | 0.42 | 0.75 | 26 | empty |
| 5 | 111 | 0.41 | 0.77 | 25 | empty |
Modifications
Observed in the structure: 11 disulfide, 4 glycan (disulfide, N-glycosylation).
Compared structures
- 6E18 · Crystal structure of Chlamydomonas reinhardtii HAP2 ectodomain provides structural… · the same entry in another collection · chain A against A, TM-score 1.00
- A4GRC6 · AlphaFold monomer V2.0 prediction for hapless 2 (A4GRC6) · a predicted model of the same protein · 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 A4GRC6
- Elsewhere: RCSB PDB 6E18 · PDBe 6E18 · UniProt A4GRC6
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