Research workbench
Crystal structure of alpha-amino-beta-carboxymuconate-epsilon- semialdehyde-decarboxylase (acmsd)
Analyse Crystal structure of alpha-amino-beta-carboxymuconate-epsilon… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2HBV
- Type
- protein
- Length
- 661 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 2-amino-3-carboxymuconate 6-semialdehyde decarboxylase
- EC
- 4.1.1.45
- UniProt
- Q83V25
- Ligands
- ZN, MG
- Pockets
- 5 · best druggability 0.65
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 2-amino-3-carboxymuconate 6-semialdehyde decarboxylase (EC 4.1.1.45) | protein | 331 | 47% helix, 16% strand | Q83V25 |
| B | 2-amino-3-carboxymuconate 6-semialdehyde decarboxylase (EC 4.1.1.45) | protein | 330 | 44% helix, 13% strand | Q83V25 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 416 | 0.65 | 0.78 | 35 | ZN |
| 2 | 315 | 0.58 | 0.76 | 31 | empty |
| 3 | 97 | 0.38 | 0.76 | 20 | empty |
| 4 | 67 | 0.36 | 0.78 | 22 | empty |
| 5 | 86 | 0.36 | 0.75 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 2573 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
- 2HBV · Crystal Structure of alpha-Amino-beta-Carboxymuconate-epsilon-Semialdehyde-Decarboxylase… · 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 Q83V25
- Elsewhere: RCSB PDB 2HBV · PDBe 2HBV · UniProt Q83V25
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.