MolNFT v1 · #171967 · protein
Crystal structure of chaetomium thermophilum NAA20 in complex with a bisubstrate analogue
6ZMP · N-terminal acetyltransferase-like protein: “Crystal structure of chaetomium thermophilum NAA20 in complex with a bisubstrate analogue”. X-ray diffraction, 1 ligand (CMC), 4 pockets (best druggability 0.81). MolNFT v1 #171967 on…
- PDB
- 6ZMP
- Type
- protein
- Length
- 388 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N-terminal acetyltransferase-like protein; Cmc-met-asp-glu-leu
- UniProt
- G0SGG4
- Ligands
- CMC
- Pockets
- 4 · best druggability 0.81
Structure
x-ray diffraction · 2 distinct chains · 30% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | N-terminal acetyltransferase-like protein | protein | 190 | 31% helix, 29% strand | G0SGG4 |
| C, D | Cmc-met-asp-glu-leu | protein | 4 | 0% helix, 0% strand | — |
Ligands and binding sites
- CMC · Carboxymethyl coenzyme *A · ligand · 2 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 942 | 0.81 | 0.82 | 93 | CMC |
| 2 | 125 | 0.56 | 0.83 | 24 | empty |
| 3 | 107 | 0.55 | 0.84 | 25 | empty |
| 4 | 212 | 0.52 | 0.77 | 26 | empty |
Interfaces
3 interfaces between chains.
- A–B · 551 Ų buried · 4 hydrogen bonds · protein-protein
- A–C · 490 Ų buried · 10 hydrogen bonds · protein-protein
- B–D · 480 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent (covalent ligand).
Compared structures
- 6ZMP · Crystal structure of Chaetomium thermophilum Naa20 in complex with a bisubstrate analogue · the same entry in another collection · chain A against A, 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 G0SGG4
- Elsewhere: RCSB PDB 6ZMP · PDBe 6ZMP · UniProt G0SGG4
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