MolNFT v1 · #31792 · protein
Crystal structure of human udp-glucoronic acid decarboxylase
2B69 · Udp-glucuronate decarboxylase 1: “Crystal structure of human udp-glucoronic acid decarboxylase”. X-ray diffraction, 2 ligands (UDP, NAD), 1 pocket (best druggability 0.85). MolNFT v1 #31792 on GenesisL1: 3D structure, binding sites…
- PDB
- 2B69
- Type
- protein
- Length
- 312 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Udp-glucuronate decarboxylase 1
- EC
- 4.1.1.35
- UniProt
- Q8NBZ7
- Ligands
- UDP, NAD
- Pockets
- 1 · best druggability 0.85
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-glucuronate decarboxylase 1 (EC 4.1.1.35) | protein | 312 | 42% helix, 19% strand | Q8NBZ7 |
Ligands and binding sites
- UDP · Uridine-5'-diphosphate · ligand · 2 copies · chains A
- NAD · Nicotinamide-adenine-dinucleotide · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 604 | 0.85 | 0.90 | 72 | NAD, UDP |
Modifications
Observed in the structure: 10 modified (engineered).
Compared structures
- 2B69 · Crystal Structure of Human UDP-glucoronic acid decarboxylase · the same entry in another collection · chain A against A, TM-score 1.00
- Q8NBZ7 · AlphaFold monomer V2.0 prediction for udp-glucuronic acid decarboxylase 1 (Q8NBZ7) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q8NBZ7
- Elsewhere: RCSB PDB 2B69 · PDBe 2B69 · UniProt Q8NBZ7
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