MolNFT v1 · #46536 · protein
Tyrosine ammonia-lyase from rhodobacter sphaeroides (HIS89PHE variant), bound to 2-aminoindan-2-phosphonic acid
2O7E · Putative histidine ammonia-lyase: “Tyrosine ammonia-lyase from rhodobacter sphaeroides (HIS89PHE variant), bound to 2-aminoindan-2-phosphonic…”. X-ray diffraction, 1 ligand (PMI), 20 pockets (best druggability 0.82). MolNFT v1…
- PDB
- 2O7E
- Type
- protein
- Length
- 4,114 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative histidine ammonia-lyase
- EC
- 4.3.1.-
- UniProt
- Q3IWB0
- Ligands
- PMI
- Pockets
- 20 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 57% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Putative histidine ammonia-lyase (EC 4.3.1.-) | protein | 515 | 56% helix, 7% strand | Q3IWB0 |
| C, D, E, F, G, H | Putative histidine ammonia-lyase (EC 4.3.1.-) | protein | 514 | 57% helix, 7% strand | Q3IWB0 |
Ligands and binding sites
- PMI · (2-amino-2,3-dihydro-1H-inden-2-yl)phosphonic acid · ligand · 8 copies · chains A, B, D, C, E, F, H, G
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 167 | 0.82 | 0.97 | 46 | empty |
| 2 | 138 | 0.79 | 0.97 | 28 | empty |
| 3 | 259 | 0.78 | 0.90 | 49 | PMI |
| 4 | 134 | 0.77 | 0.96 | 26 | empty |
| 5 | 137 | 0.77 | 0.96 | 26 | empty |
Interfaces
18 interfaces between chains.
- A–D · 4692 Ų buried · 69 hydrogen bonds · protein-protein
- F–G · 4682 Ų buried · 72 hydrogen bonds · protein-protein
- E–H · 4671 Ų buried · 71 hydrogen bonds · protein-protein
- B–C · 4660 Ų buried · 69 hydrogen bonds · protein-protein
- G–H · 3154 Ų buried · 53 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 covalent, 8 modified (covalent ligand, nonstandard).
Compared structures
- Q3IWB0 · AlphaFold monomer V2.0 prediction for tyrosine ammonia-lyase (Q3IWB0) · a predicted model of the same protein · chain A against A, TM-score 1.00
- 2O7E · Tyrosine ammonia-lyase from Rhodobacter sphaeroides (His89Phe variant), bound to… · 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 Q3IWB0
- Elsewhere: RCSB PDB 2O7E · PDBe 2O7E · UniProt Q3IWB0
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