Research workbench
Cryo-EM structure of arabidopsis thaliana complex-I (membrane tip)
Analyse Cryo-EM structure of arabidopsis thaliana complex-I (membrane tip) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7AQW
- Type
- protein
- Length
- 1,580 residues
- Chains
- 13
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- B5TM94, B5TM93, P53665, Q8VZT9, Q9SLC8, A0A178W1I8, Q8LDK3, O64725, Q9FGK0, A0A178VZI4, Q945M1, Q9SKC9, Q94C12
- Ligands
- PTY, PC7, 8Q1
Structure
electron microscopy · 13 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| L | — | protein | 589 | — | B5TM94 |
| M | — | protein | 225 | — | B5TM93 |
| T | — | protein | 84 | — | P53665 |
| c | — | protein | 76 | — | Q8VZT9 |
| g | — | protein | 75 | — | Q9SLC8 |
| i | — | protein | 15 | — | A0A178W1I8 |
| j | — | protein | 51 | — | Q8LDK3 |
| k | — | protein | 47 | — | O64725 |
| l | — | protein | 66 | — | Q9FGK0 |
| m | — | protein | 70 | — | A0A178VZI4 |
| n | — | protein | 109 | — | Q945M1 |
| o | — | protein | 80 | — | Q9SKC9 |
| p | — | protein | 93 | — | Q94C12 |
Ligands and binding sites
- PTY · Phosphatidylethanolamine · ligand · chains M, g
- PC7 · (7S)-4-hydroxy-N,N,N-trimethyl-9-oxo-7-[(palmitoyloxy) methyl]-3,5,8-trioxa-4-phosphahexacosan-1-aminium 4-oxide · ligand · chains L, M, c
- 8Q1 · S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy) butanoyl]-beta-alanyl}amino)ethyl] dodecanethioate · ligand · chains T, n
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7AQW · Cryo-EM structure of Arabidopsis thaliana Complex-I (membrane tip) · the same entry in another collection · chain p against p, 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 B5TM94
- Every structure of UniProt B5TM93
- Every structure of UniProt P53665
- Every structure of UniProt Q8VZT9
- Every structure of UniProt Q9SLC8
- Every structure of UniProt A0A178W1I8
- Every structure of UniProt Q8LDK3
- Every structure of UniProt O64725
- Every structure of UniProt Q9FGK0
- Every structure of UniProt A0A178VZI4
- Every structure of UniProt Q945M1
- Every structure of UniProt Q9SKC9
- Every structure of UniProt Q94C12
- Elsewhere: RCSB PDB 7AQW · PDBe 7AQW · UniProt B5TM94 · UniProt B5TM93 · UniProt P53665 · UniProt Q8VZT9 · UniProt Q9SLC8 · UniProt A0A178W1I8 · UniProt Q8LDK3 · UniProt O64725 · UniProt Q9FGK0 · UniProt A0A178VZI4 · UniProt Q945M1 · UniProt Q9SKC9 · UniProt Q94C12
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