Research workbench
Structure of a lys-hct mutant from coffea canephora (crystal form 2)
Analyse Structure of a lys-hct mutant from coffea canephora (crystal form 2) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4G2M
- Type
- protein
- Length
- 419 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hydroxycinnamoyl-CoA SHIKIMATE/QUINATE hydroxycinnamoyltransferase
- EC
- 2.3.1.99
- UniProt
- A4ZKE4
- Pockets
- 4 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hydroxycinnamoyl-CoA SHIKIMATE/QUINATE hydroxycinnamoyltransferase (EC 2.3.1.99) | protein | 419 | 32% helix, 23% strand | A4ZKE4 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 720 | 0.82 | 0.86 | 72 | empty |
| 2 | 65 | 0.33 | 0.76 | 19 | empty |
| 3 | 74 | 0.31 | 0.74 | 19 | empty |
| 4 | 51 | 0.27 | 0.74 | 13 | empty |
Modifications
Observed in the structure: 1 modified (oxidation).
Compared structures
- 4G2M · Structure of a Lys-HCT mutant from Coffea canephora (Crystal form 2) · 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 4G2M · PDBe 4G2M · UniProt A4ZKE4
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