MolNFT v1 · #100313 · protein
Beta-alanyl-COA:AMMONIA lyase from clostridium propionicum
4MTU · Beta-alanyl-COA:AMMONIA lyase 2: “Beta-alanyl-COA:AMMONIA lyase from clostridium propionicum”. X-ray diffraction, 2 ligands (ZN, SO4). MolNFT v1 #100313 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4MTU
- Type
- protein
- Length
- 143 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-alanyl-COA:AMMONIA lyase 2
- UniProt
- Q6KC22
- Ligands
- ZN, SO4
Structure
x-ray diffraction · 1 distinct chain · 20% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-alanyl-COA:AMMONIA lyase 2 | protein | 143 | 20% helix, 47% strand | Q6KC22 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 4MTU · beta-Alanyl-CoA:Ammonia Lyase from Clostridium propionicum · 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 Q6KC22
- Elsewhere: RCSB PDB 4MTU · PDBe 4MTU · UniProt Q6KC22
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