Research workbench
Structure of pkbalpha pH domain in complex with a novel inositol headgroup surrogate, benzene 1,2,3,4- tetrakisphosphate
Analyse Structure of pkbalpha pH domain in complex with a novel inositol headgroup… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2UVM
- Type
- protein
- Length
- 115 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Rac-alpha SERINE/THREONINE-protein kinase
- EC
- 2.7.11.1
- UniProt
- P31749
- Ligands
- GVF, NA
Structure
x-ray diffraction · 1 distinct chain · 24% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Rac-alpha SERINE/THREONINE-protein kinase (EC 2.7.11.1) | protein | 115 | 24% helix, 43% strand | P31749 |
Ligands and binding sites
- GVF · Benzene-1,2,3,4-tetrayl tetrakis[dihydrogen (phosphate)] · ligand · chains A
- NA · Sodium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2UVM · Structure of PKBalpha PH domain in complex with a novel inositol headgroup surrogate… · the same entry in another collection · chain A against A, TM-score 1.00
- P31749 · AlphaFold monomer V2.0 prediction for rac-alpha SERINE/THREONINE- protein kinase (P31749) · a predicted model of the same protein · chain A against A, TM-score 0.91
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 P31749
- Elsewhere: RCSB PDB 2UVM · PDBe 2UVM · UniProt P31749
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