MolNFT v1 · #18235 · protein
Three-dimensional structure of the bifunctional enzyme phosphoribosylanthranilate isomerase: indoleglycerolphosphate synthase from escherichia COLI refined at 2.0 ångströms resolution
1PII · N-(5'PHOSPHORIBOSYL)ANTHRANILATE isomerase: “Three-dimensional structure of the bifunctional enzyme phosphoribosylanthranilate isomerase…”. X-ray diffraction, 1 ligand (PO4), 4 pockets (best druggability 0.75). MolNFT v1 #18235 on…
- PDB
- 1PII
- Type
- protein
- Length
- 452 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N-(5'PHOSPHORIBOSYL)ANTHRANILATE isomerase
- EC
- 4.1.1.48
- UniProt
- P00909
- Ligands
- PO4
- Pockets
- 4 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N-(5'PHOSPHORIBOSYL)ANTHRANILATE isomerase (EC 4.1.1.48) | protein | 452 | 38% helix, 20% strand | P00909 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 131 | 0.75 | 0.94 | 29 | PO4 |
| 2 | 150 | 0.68 | 0.89 | 28 | PO4 |
| 3 | 97 | 0.34 | 0.74 | 23 | empty |
| 4 | 53 | 0.31 | 0.77 | 16 | empty |
Compared structures
- 1PII · Three-dimensional structure of the bifunctional enzyme phosphoribosylanthranilate… · the same entry in another collection · chain A against A, TM-score 1.00
- P00909 · AlphaFold monomer V2.0 prediction for tryptophan biosynthesis protein trpcf (P00909) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P00909
- Elsewhere: RCSB PDB 1PII · PDBe 1PII · UniProt P00909
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.