MolNFT v1 · #177726 · protein
Crystal structure of L-histidine decarboxylase (C57S/C101V/C282V mutant) from photobacterium phosphoreum
7ERV: “Crystal structure of L-histidine decarboxylase (C57S/C101V/C282V mutant) from photobacterium phosphoreum”. X-ray diffraction, 2 pockets (best druggability 0.35). MolNFT v1 #177726 on GenesisL1: 3D structure, binding sites and…
- PDB
- 7ERV
- Type
- protein
- Length
- 374 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histidine decarboxylase
- EC
- 4.1.1.22
- UniProt
- Q1JU62
- Pockets
- 2 · best druggability 0.35
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histidine decarboxylase (EC 4.1.1.22) | protein | 374 | 42% helix, 14% strand | Q1JU62 |
Ligands and binding sites
- IMD · Imidazole · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 65 | 0.35 | 0.77 | 23 | empty |
| 2 | 92 | 0.33 | 0.74 | 18 | empty |
Modifications
Observed in the structure: 1 modified (cofactor).
Compared structures
- 7ERV · Crystal structure of L-histidine decarboxylase (C57S/C101V/C282V mutant) from… · 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 Q1JU62
- Elsewhere: RCSB PDB 7ERV · PDBe 7ERV · UniProt Q1JU62
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