MolNFT v1 · #183719 · protein
ABC transporter nosdfy, nucleotide-free in gdn
7O0Y: “ABC transporter nosdfy, nucleotide-free in gdn”. Electron microscopy, 1 ligand (MG). MolNFT v1 #183719 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7O0Y
- Type
- protein
- Length
- 1,514 residues
- Chains
- 5
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P19843, P19844, P19845
- Ligands
- MG
Structure
electron microscopy · 5 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 402 | — | P19843 |
| B | — | protein | 299 | — | P19844 |
| C | — | protein | 298 | — | P19844 |
| D | — | protein | 267 | — | P19845 |
| E | — | protein | 248 | — | P19845 |
Ligands and binding sites
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7O0Y · ABC transporter NosDFY, nucleotide-free in GDN · the same entry in another collection · chain E against E, TM-score 1.00
- P19844 · AlphaFold monomer V2.0 prediction for probable ABC transporter ATP- binding protein nosf… · a predicted model of the same protein · chain C against A, TM-score 0.97
- P19843 · AlphaFold monomer V2.0 prediction for probable ABC transporter binding protein nosd… · a predicted model of the same protein · chain A 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 D against A, TM-score 0.94
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 P19843
- Every structure of UniProt P19844
- Every structure of UniProt P19845
- Elsewhere: RCSB PDB 7O0Y · PDBe 7O0Y · UniProt P19843 · UniProt P19844 · UniProt P19845
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