MolNFT v1 · #156594 · protein
Crystal structure of the high-affinity copper transporter CTR1
6M97 · Chimera protein of high affinity copper uptake protein 1…: “Crystal structure of the high-affinity copper transporter CTR1”. X-ray diffraction, 2 ligands (TBR, ZN), 1 pocket (best druggability 0.55). MolNFT v1 #156594 on GenesisL1…
- PDB
- 6M97
- Type
- protein
- Length
- 208 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chimera protein of high affinity copper uptake protein 1 and soluble cytochrome B562
- UniProt
- C0HAK2, P0ABE7
- Ligands
- TBR, ZN
- Pockets
- 1 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 76% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chimera protein of high affinity copper uptake protein 1 and soluble cytochrome B562 | protein | 208 | 76% helix, 3% strand | C0HAK2, P0ABE7 |
Ligands and binding sites
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 | 251 | 0.55 | 0.77 | 35 | empty |
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 C0HAK2
- Every structure of UniProt P0ABE7
- Elsewhere: RCSB PDB 6M97 · PDBe 6M97 · UniProt C0HAK2 · UniProt P0ABE7
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