Research workbench
Phosphoribosyl anthranilate isomerase from thermococcus kodakaraensis
Analyse Phosphoribosyl anthranilate isomerase from thermococcus kodakaraensis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5LHF
- Type
- protein
- Length
- 417 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N-(5'-PHOSPHORIBOSYL)ANTHRANILATE isomerase
- EC
- 5.3.1.24
- UniProt
- Q9YGB1
- Ligands
- NA, CL
- Pockets
- 3 · best druggability 0.52
Structure
x-ray diffraction · 2 distinct chains · 44% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N-(5'-PHOSPHORIBOSYL)ANTHRANILATE isomerase (EC 5.3.1.24) | protein | 208 | 44% helix, 21% strand | Q9YGB1 |
| B | N-(5'-PHOSPHORIBOSYL)ANTHRANILATE isomerase (EC 5.3.1.24) | protein | 209 | 44% helix, 21% strand | Q9YGB1 |
Ligands and binding sites
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 | 217 | 0.52 | 0.77 | 26 | empty |
| 2 | 207 | 0.52 | 0.77 | 27 | empty |
| 3 | 230 | 0.52 | 0.76 | 31 | empty |
Interfaces
1 interface between chains.
- A–B · 341 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 5LHF · Phosphoribosyl anthranilate isomerase from Thermococcus kodakaraensis · the same entry in another collection · chain A against A, TM-score 1.00
- Q9YGB1 · AlphaFold monomer V2.0 prediction for N-(5'-PHOSPHORIBOSYL)ANTHRANILATE isomerase (Q9YGB1) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 Q9YGB1
- Elsewhere: RCSB PDB 5LHF · PDBe 5LHF · UniProt Q9YGB1
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