Research workbench
Crystal structure of selenomethionine incorporated holo diaminopropionate ammonia lyase from escherichia COLI
Analyse Crystal structure of selenomethionine incorporated holo diaminopropionate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4D9G
- Type
- protein
- Length
- 781 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative diaminopropionate ammonia-lyase
- EC
- 4.3.1.15
- UniProt
- P66899
- Pockets
- 3 · best druggability 0.61
Structure
x-ray diffraction · 2 distinct chains · 46% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative diaminopropionate ammonia-lyase (EC 4.3.1.15) | protein | 389 | 46% helix, 15% strand | P66899 |
| B | Putative diaminopropionate ammonia-lyase (EC 4.3.1.15) | protein | 392 | 46% helix, 15% strand | P66899 |
Ligands and binding sites
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 325 | 0.61 | 0.78 | 56 | TRS |
| 2 | 111 | 0.54 | 0.83 | 25 | TRS |
| 3 | 182 | 0.51 | 0.78 | 37 | empty |
Interfaces
1 interface between chains.
- A–B · 1101 Ų buried · 29 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 28 modified, 2 disulfide (engineered, disulfide, artifact, cofactor).
Compared structures
- 4D9G · Crystal structure of Selenomethionine incorporated holo Diaminopropionate ammonia lyase… · the same entry in another collection · chain A against A, TM-score 1.00
- P66899 · AlphaFold monomer V2.0 prediction for diaminopropionate ammonia-lyase (P66899) · a predicted model of the same protein · 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 P66899
- Elsewhere: RCSB PDB 4D9G · PDBe 4D9G · UniProt P66899
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