Research workbench
Crystal structure of mutually generated monomers of dimeric phosphoribosylantranilate isomerase from thermotoga maritima
Analyse Crystal structure of mutually generated monomers of dimeric… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1DL3
- Type
- protein
- Length
- 385 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (phosphoribosylantranilate isomerase)
- EC
- 5.3.1.24
- UniProt
- Q56320
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.53
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (phosphoribosylantranilate isomerase) (EC 5.3.1.24) | protein | 191 | 38% helix, 24% strand | Q56320 |
| B | Protein (phosphoribosylantranilate isomerase) (EC 5.3.1.24) | protein | 194 | 40% helix, 22% strand | Q56320 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 220 | 0.53 | 0.77 | 24 | SO4 |
| 2 | 175 | 0.47 | 0.76 | 22 | SO4 |
Compared structures
- 1DL3 · Crystal structure of mutually generated monomers of dimeric phosphoribosylantranilate… · the same entry in another collection · chain A against A, TM-score 1.00
- Q56320 · AlphaFold monomer V2.0 prediction for N-(5'-PHOSPHORIBOSYL)ANTHRANILATE isomerase (Q56320) · 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 Q56320
- Elsewhere: RCSB PDB 1DL3 · PDBe 1DL3 · UniProt Q56320
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.