Research workbench
Mutation in the trinuclear site of cota-laccase: H493C mutant, pH 8.0
Analyse Mutation in the trinuclear site of cota-laccase: H493C mutant, pH 8.0 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5ZLL
- Type
- protein
- Length
- 503 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Spore coat protein a
- UniProt
- P07788
- Ligands
- CU
- Pockets
- 5 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 8% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Spore coat protein a | protein | 503 | 8% helix, 41% strand | P07788 |
Ligands and binding sites
- CU · Copper (II) ion · metal · 3 copies · chains A
- EDO · 1,2-ethanediol · additive · 4 copies · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 178 | 0.55 | 0.80 | 33 | empty |
| 2 | 176 | 0.53 | 0.79 | 22 | empty |
| 3 | 122 | 0.44 | 0.77 | 25 | empty |
| 4 | 111 | 0.36 | 0.73 | 21 | empty |
| 5 | 50 | 0.24 | 0.73 | 18 | EDO |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 5ZLL · Mutation in the trinuclear site of CotA-laccase: H493C mutant, PH 8.0 · the same entry in another collection · chain A against A, TM-score 1.00
- P07788 · AlphaFold monomer V2.0 prediction for spore coat protein a (P07788) · 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 P07788
- Elsewhere: RCSB PDB 5ZLL · PDBe 5ZLL · UniProt P07788
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