MolNFT v1 · #29872 · protein
Structure of the EEF2-eta-btad complex
1ZM4 · Elongation factor 2: “Structure of the EEF2-eta-btad complex”. X-ray diffraction, 1 ligand (TAD), 20 pockets (best druggability 0.81). MolNFT v1 #29872 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1ZM4
- Type
- protein
- Length
- 3,090 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Elongation factor 2; Exotoxin a
- EC
- 2.4.2.36
- UniProt
- P32324
- Ligands
- TAD
- Pockets
- 20 · best druggability 0.81
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E | Elongation factor 2 | protein | 823 | 36% helix, 25% strand | P32324 |
| B, D, F | Exotoxin a (EC 2.4.2.36) | protein | 207 | 26% helix, 23% strand | — |
Ligands and binding sites
- TAD · Beta-methylene-thiazole-4-carboxyamide-adenine dinucleotide · ligand · 3 copies · chains B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1142 | 0.81 | 0.82 | 101 | empty |
| 2 | 521 | 0.79 | 0.85 | 64 | empty |
| 3 | 971 | 0.79 | 0.80 | 81 | empty |
| 4 | 1170 | 0.77 | 0.79 | 124 | empty |
| 5 | 905 | 0.77 | 0.80 | 114 | empty |
Interfaces
6 interfaces between chains.
- C–D · 886 Ų buried · 5 hydrogen bonds · protein-protein
- E–F · 873 Ų buried · 9 hydrogen bonds · protein-protein
- A–B · 851 Ų buried · 8 hydrogen bonds · protein-protein
- A–F · 327 Ų buried · 6 hydrogen bonds · protein-protein
- B–C · 311 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 modified (nonstandard).
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 P32324
- Elsewhere: RCSB PDB 1ZM4 · PDBe 1ZM4 · UniProt P32324
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