Research workbench
Crystal structure of cobb AC3(A76G,Y92A, I131L, V187Y) in complex with H4K16-acetyl peptide
Analyse Crystal structure of cobb AC3(A76G,Y92A, I131L, V187Y) in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6RXS
- Type
- protein
- Length
- 226 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- NAD-dependent protein deacylase; Histone H4
- EC
- 3.5.1.-
- UniProt
- P75960, P62805
- Ligands
- ZN
- Pockets
- 2 · best druggability 0.66
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NAD-dependent protein deacylase (EC 3.5.1.-) | protein | 218 | 36% helix, 19% strand | P75960 |
| B | Histone H4 | protein | 8 | 0% helix, 25% strand | P62805 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 216 | 0.66 | 0.84 | 40 | empty |
| 2 | 116 | 0.44 | 0.78 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 630 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (acetylation).
Compared structures
- 6RXS · Crystal structure of CobB Ac3(A76G,Y92A, I131L, V187Y) in complex with H4K16-Acetyl… · the same entry in another collection · chain A against A, TM-score 1.00
- P75960 · AlphaFold monomer V2.0 prediction for NAD-dependent protein deacylase (P75960) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 P75960
- Every structure of UniProt P62805
- Elsewhere: RCSB PDB 6RXS · PDBe 6RXS · UniProt P75960 · UniProt P62805
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