Research workbench
Structure of the SSL1 laccase mutant H99N with depleted type-2 copper ion
Analyse Structure of the SSL1 laccase mutant H99N with depleted type-2 copper ion in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4UAH
- Type
- protein
- Length
- 819 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Copper oxidase
- UniProt
- B5HSR1
- Ligands
- CU
- Pockets
- 10 · best druggability 0.85
Structure
x-ray diffraction · 3 distinct chains · 6% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Copper oxidase | protein | 272 | 6% helix, 42% strand | B5HSR1 |
| B | Copper oxidase | protein | 271 | 6% helix, 42% strand | B5HSR1 |
| C | Copper oxidase | protein | 276 | 6% helix, 41% strand | B5HSR1 |
Ligands and binding sites
- CU · Copper (II) ion · metal · 9 copies · chains A, C, B
- GOL · Glycerol · additive · 3 copies · chains B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 415 | 0.85 | 0.93 | 67 | GOL |
| 2 | 53 | 0.69 | 0.98 | 19 | empty |
| 3 | 54 | 0.68 | 0.97 | 19 | empty |
| 4 | 187 | 0.56 | 0.80 | 37 | empty |
| 5 | 178 | 0.55 | 0.80 | 36 | GOL |
Interfaces
3 interfaces between chains.
- A–C · 1940 Ų buried · 41 hydrogen bonds · protein-protein
- A–B · 1936 Ų buried · 37 hydrogen bonds · protein-protein
- B–C · 1797 Ų buried · 39 hydrogen bonds · protein-protein
Compared structures
- 4UAH · Structure of the Ssl1 laccase mutant H99N with depleted type-2 copper ion · the same entry in another collection · chain B against B, 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 B5HSR1
- Elsewhere: RCSB PDB 4UAH · PDBe 4UAH · UniProt B5HSR1
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