MolNFT v1 · #99297 · protein
Crystal structure of adenine phosphoribosyltransferase from thermoanaerobacter pseudethanolicus atcc 33223, nysgrc target 029700.
4LZA: “Crystal structure of adenine phosphoribosyltransferase from thermoanaerobacter pseudethanolicus atcc 33223…”. X-ray diffraction, 1 ligand (CL), 2 pockets (best druggability 0.65). MolNFT v1 #99297 on GenesisL1: 3D structure, binding…
- PDB
- 4LZA
- Type
- protein
- Length
- 340 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Adenine phosphoribosyltransferase
- EC
- 2.4.2.7
- UniProt
- B0K969
- Ligands
- CL
- Pockets
- 2 · best druggability 0.65
Structure
x-ray diffraction · 2 distinct chains · 32% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Adenine phosphoribosyltransferase (EC 2.4.2.7) | protein | 168 | 33% helix, 33% strand | B0K969 |
| B | Adenine phosphoribosyltransferase (EC 2.4.2.7) | protein | 172 | 32% helix, 35% strand | B0K969 |
Ligands and binding sites
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 395 | 0.65 | 0.79 | 34 | empty |
| 2 | 334 | 0.59 | 0.77 | 31 | empty |
Interfaces
1 interface between chains.
- A–B · 1642 Ų buried · 18 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 modified (engineered).
Compared structures
- 4LZA · Crystal structure of adenine phosphoribosyltransferase from Thermoanaerobacter… · the same entry in another collection · chain A against A, TM-score 1.00
- B0K969 · AlphaFold monomer V2.0 prediction for adenine phosphoribosyltransferase (B0K969) · 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 B0K969
- Elsewhere: RCSB PDB 4LZA · PDBe 4LZA · UniProt B0K969
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