Research workbench
Crystal structure of phenylalanine ammonia-lyase from anabaena variabilis
Analyse Crystal structure of phenylalanine ammonia-lyase from anabaena variabilis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2NYN
- Type
- protein
- Length
- 2,048 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- PHENYLALANINE/HISTIDINE ammonia-lyase
- EC
- 4.3.1.3
- UniProt
- Q3M5Z3
- Pockets
- 19 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 60% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | PHENYLALANINE/HISTIDINE ammonia-lyase (EC 4.3.1.3) | protein | 512 | 60% helix, 7% strand | Q3M5Z3 |
Pockets
19 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 65 | 0.72 | 0.97 | 24 | empty |
| 2 | 51 | 0.72 | 0.99 | 20 | empty |
| 3 | 51 | 0.68 | 0.97 | 23 | empty |
| 4 | 506 | 0.66 | 0.77 | 42 | empty |
| 5 | 559 | 0.66 | 0.76 | 42 | empty |
Interfaces
6 interfaces between chains.
- A–D · 3523 Ų buried · 58 hydrogen bonds · protein-protein
- B–C · 3519 Ų buried · 62 hydrogen bonds · protein-protein
- A–B · 3201 Ų buried · 37 hydrogen bonds · protein-protein
- C–D · 3196 Ų buried · 36 hydrogen bonds · protein-protein
- A–C · 390 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (nonstandard).
Compared structures
- 2NYN · Crystal structure of phenylalanine ammonia-lyase from Anabaena variabilis · the same entry in another collection · chain C against C, TM-score 1.00
- Q3M5Z3 · AlphaFold monomer V2.0 prediction for phenylalanine ammonia-lyase (Q3M5Z3) · 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 Q3M5Z3
- Elsewhere: RCSB PDB 2NYN · PDBe 2NYN · UniProt Q3M5Z3
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