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Crystal structure of human glcat-S apo form
Analyse Crystal structure of human glcat-S apo form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2D0J
- Type
- protein
- Length
- 967 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Galactosylgalactosylxylosylprotein 3-beta- glucuronosyltransferase 2
- EC
- 2.4.1.135
- UniProt
- Q9NPZ5
- Pockets
- 11 · best druggability 0.69
Structure
x-ray diffraction · 2 distinct chains · 28% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Galactosylgalactosylxylosylprotein 3-beta- glucuronosyltransferase 2 (EC 2.4.1.135) | protein | 242 | 28% helix, 23% strand | Q9NPZ5 |
| D | Galactosylgalactosylxylosylprotein 3-beta- glucuronosyltransferase 2 (EC 2.4.1.135) | protein | 241 | 28% helix, 22% strand | Q9NPZ5 |
Pockets
11 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 609 | 0.69 | 0.78 | 46 | empty |
| 2 | 596 | 0.69 | 0.78 | 55 | empty |
| 3 | 472 | 0.67 | 0.79 | 49 | empty |
| 4 | 489 | 0.66 | 0.78 | 48 | empty |
| 5 | 492 | 0.65 | 0.77 | 49 | empty |
Interfaces
3 interfaces between chains.
- A–B · 2324 Ų buried · 52 hydrogen bonds · protein-protein
- C–D · 2269 Ų buried · 44 hydrogen bonds · protein-protein
- A–D · 447 Ų buried · 6 hydrogen bonds · protein-protein
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 Q9NPZ5
- Elsewhere: RCSB PDB 2D0J · PDBe 2D0J · UniProt Q9NPZ5
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