Research workbench
Structure of a lys-hct mutant from coffea canephora (crystal form 1)
Analyse Structure of a lys-hct mutant from coffea canephora (crystal form 1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4G22
- Type
- protein
- Length
- 837 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hydroxycinnamoyl-CoA SHIKIMATE/QUINATE hydroxycinnamoyltransferase
- EC
- 2.3.1.133
- UniProt
- A4ZKE4
- Ligands
- CL
- Pockets
- 11 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 31% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hydroxycinnamoyl-CoA SHIKIMATE/QUINATE hydroxycinnamoyltransferase (EC 2.3.1.133) | protein | 419 | 31% helix, 23% strand | A4ZKE4 |
| B | Hydroxycinnamoyl-CoA SHIKIMATE/QUINATE hydroxycinnamoyltransferase (EC 2.3.1.133) | protein | 418 | 32% helix, 22% strand | A4ZKE4 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 360 | 0.76 | 0.86 | 46 | GOL |
| 2 | 354 | 0.76 | 0.86 | 40 | GOL |
| 3 | 1075 | 0.75 | 0.78 | 75 | empty |
| 4 | 104 | 0.57 | 0.85 | 25 | empty |
| 5 | 104 | 0.42 | 0.77 | 24 | empty |
Interfaces
1 interface between chains.
- A–B · 259 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (oxidation).
Compared structures
- 4G22 · Structure of a Lys-HCT mutant from Coffea canephora (Crystal form 1) · 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 A4ZKE4
- Elsewhere: RCSB PDB 4G22 · PDBe 4G22 · UniProt A4ZKE4
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