Research workbench
Cinnamate 4-hydroxylase (C4H1) from sorghum bicolor
Analyse Cinnamate 4-hydroxylase (C4H1) from sorghum bicolor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6VBY
- Type
- protein
- Length
- 470 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cinnamic acid 4-hydroxylase
- EC
- 1.14.13.11
- UniProt
- Q94IP1
- Ligands
- HEM
- Pockets
- 4 · best druggability 0.85
Structure
x-ray diffraction · 1 distinct chain · 56% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cinnamic acid 4-hydroxylase (EC 1.14.13.11) | protein | 470 | 56% helix, 10% strand | Q94IP1 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
- GOL · Glycerol · additive · 2 copies · chains A
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 931 | 0.85 | 0.86 | 103 | EPE, HEM, GOL |
| 2 | 140 | 0.47 | 0.77 | 18 | empty |
| 3 | 63 | 0.34 | 0.77 | 13 | empty |
| 4 | 66 | 0.32 | 0.76 | 17 | empty |
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 Q94IP1
- Elsewhere: RCSB PDB 6VBY · PDBe 6VBY · UniProt Q94IP1
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