MolNFT v1 · #141866 · protein
Mutation in the trinuclear site of cota-laccase: H491C mutant, pH 8.0
5ZLM · Spore coat protein a: “Mutation in the trinuclear site of cota-laccase: H491C mutant, pH 8.0”. X-ray diffraction, 1 ligand (CU), 5 pockets (best druggability 0.54). MolNFT v1 #141866 on GenesisL1: 3D structure, binding sites and…
- PDB
- 5ZLM
- Type
- protein
- Length
- 502 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 0.54
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 | 502 | 8% helix, 41% strand | P07788 |
Ligands and binding sites
- CU · Copper (II) ion · metal · 3 copies · chains A
- EDO · 1,2-ethanediol · additive · 9 copies · chains A
- GOL · Glycerol · additive · 2 copies · 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 | 218 | 0.54 | 0.78 | 39 | empty |
| 2 | 155 | 0.52 | 0.79 | 22 | empty |
| 3 | 119 | 0.48 | 0.80 | 26 | EDO |
| 4 | 113 | 0.36 | 0.73 | 22 | empty |
| 5 | 57 | 0.28 | 0.74 | 15 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 5ZLM · Mutation in the trinuclear site of CotA-laccase: H491C 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 5ZLM · PDBe 5ZLM · UniProt P07788
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