MolNFT v1 · #173346 · protein
E. COLI NADH quinone oxidoreductase hydrophilic arm
7AWT: “E. COLI NADH quinone oxidoreductase hydrophilic arm”. Electron microscopy, 4 ligands (SF4, FES, FMN). MolNFT v1 #173346 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7AWT
- Type
- protein
- Length
- 2,375 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A4P6IQ32, A0A024L1E0, A0A5A4T568, A0A037YNA7, A0A037YPU0, A0A1X3LLK1
- Ligands
- SF4, FES, FMN, MG
Structure
electron microscopy · 6 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | — | protein | 141 | — | A0A4P6IQ32 |
| D | — | protein | 589 | — | A0A024L1E0 |
| E | — | protein | 156 | — | A0A5A4T568 |
| F | — | protein | 439 | — | A0A037YNA7 |
| G | — | protein | 907 | — | A0A037YPU0 |
| I | — | protein | 143 | — | A0A1X3LLK1 |
Ligands and binding sites
- SF4 · Iron/sulfur cluster · ligand · 7 copies · chains B, D, F, G, I
- FES · Fe2/s2 (inorganic) cluster · ligand · 2 copies · chains E, G
- FMN · Flavin mononucleotide · ligand · chains F
- MG · Magnesium ion · metal · 8 copies · chains E, G, I, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7AWT · E. coli NADH qui oxidoreductase hydrophilic arm · the same entry in another collection · chain B against B, 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 A0A4P6IQ32
- Every structure of UniProt A0A024L1E0
- Every structure of UniProt A0A5A4T568
- Every structure of UniProt A0A037YNA7
- Every structure of UniProt A0A037YPU0
- Every structure of UniProt A0A1X3LLK1
- Elsewhere: RCSB PDB 7AWT · PDBe 7AWT · UniProt A0A4P6IQ32 · UniProt A0A024L1E0 · UniProt A0A5A4T568 · UniProt A0A037YNA7 · UniProt A0A037YPU0 · UniProt A0A1X3LLK1
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