MolNFT v1 · #160303 · protein
Asymmetric functions of a binuclear metal cluster within the transport pathway of the zip transition metal transporters
6PGI · Bbzip: “Asymmetric functions of a binuclear metal cluster within the transport pathway of the zip transition metal…”. X-ray diffraction, 1 ligand (CD), 1 pocket (best druggability 0.65). MolNFT v1 #160303 on GenesisL1: 3D structure…
- PDB
- 6PGI
- Type
- protein
- Length
- 230 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bbzip
- UniProt
- A0A0H3LM39
- Ligands
- CD
- Pockets
- 1 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 87% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bbzip | protein | 230 | 87% helix, 0% strand | A0A0H3LM39 |
Ligands and binding sites
- CD · Cadmium ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 258 | 0.65 | 0.82 | 50 | empty |
Compared structures
- 6PGI · Asymmetric functions of a binuclear metal cluster within the transport pathway of the ZIP… · the same entry in another collection · 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 A0A0H3LM39
- Elsewhere: RCSB PDB 6PGI · PDBe 6PGI · UniProt A0A0H3LM39
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