Research workbench
ABC transporter complex nosdfyl in gdn
Analyse ABC transporter complex nosdfyl in gdn in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7ZNQ
- Type
- protein
- Length
- 1,670 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Probable ABC transporter ATP-binding protein nosf; Probable ABC transporter permease…
- UniProt
- P19844, P19845, P19843, Q52529
- Ligands
- MG, CU, ZN
- Pockets
- 15 · best druggability 0.83
Structure
electron microscopy · 5 distinct chains · 43% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| f, F | Probable ABC transporter ATP-binding protein nosf | protein | 307 | 34% helix, 18% strand | P19844 |
| Y | Probable ABC transporter permease protein nosy | protein | 269 | 81% helix, 0% strand | P19845 |
| y | Probable ABC transporter permease protein nosy | protein | 250 | 82% helix, 0% strand | P19845 |
| D | Probable ABC transporter binding protein nosd | protein | 392 | 7% helix, 33% strand | P19843 |
| L | Copper-binding lipoprotein nosl | protein | 145 | 25% helix, 19% strand | Q52529 |
Ligands and binding sites
- MG · Magnesium ion · metal · chains D
- CU · Copper (II) ion · metal · chains D, L
- ZN · Zinc ion · metal · chains L
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 848 | 0.83 | 0.86 | 98 | empty |
| 2 | 91 | 0.77 | 0.97 | 24 | empty |
| 3 | 867 | 0.75 | 0.78 | 63 | empty |
| 4 | 826 | 0.75 | 0.79 | 62 | empty |
| 5 | 290 | 0.65 | 0.82 | 29 | empty |
Interfaces
8 interfaces between chains.
- f–F · 2446 Ų buried · 25 hydrogen bonds · protein-protein
- f–y · 1152 Ų buried · 13 hydrogen bonds · protein-protein
- D–L · 1152 Ų buried · 9 hydrogen bonds · protein-protein
- F–Y · 1132 Ų buried · 9 hydrogen bonds · protein-protein
- Y–D · 888 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 7ZNQ · ABC transporter complex NosDFYL in GDN · the same entry in another collection · chain L against L, TM-score 1.00
- P19843 · AlphaFold monomer V2.0 prediction for probable ABC transporter binding protein nosd… · a predicted model of the same protein · chain D against A, TM-score 0.96
- P19845 · AlphaFold monomer V2.0 prediction for probable ABC transporter permease protein nosy… · a predicted model of the same protein · chain y against A, TM-score 0.96
- Q52529 · AlphaFold monomer V2.0 prediction for copper-binding lipoprotein nosl (Q52529) · a predicted model of the same protein · chain L against A, TM-score 0.94
- P19844 · AlphaFold monomer V2.0 prediction for probable ABC transporter ATP- binding protein nosf… · a predicted model of the same protein · chain f against A, TM-score 0.93
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 P19844
- Every structure of UniProt P19845
- Every structure of UniProt P19843
- Every structure of UniProt Q52529
- Elsewhere: RCSB PDB 7ZNQ · PDBe 7ZNQ · UniProt P19844 · UniProt P19845 · UniProt P19843 · UniProt Q52529
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.