MolNFT v1 · #126199 · protein
Human PDK1 kinase domain in complex with an hm-peptide bound to the pif-pocket
5LVP: “Human PDK1 kinase domain in complex with an hm-peptide bound to the pif-pocket”. X-ray diffraction, 2 ligands (ATP, CL). MolNFT v1 #126199 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5LVP
- Type
- protein
- Length
- 1,135 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O15530
- Ligands
- ATP, CL
Structure
x-ray diffraction · 6 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | — | protein | 276 | — | O15530 |
| B | — | protein | 277 | — | O15530 |
| D | — | protein | 277 | — | O15530 |
| E | — | protein | 6 | — | — |
| F, G | — | protein | 8 | — | — |
| H | — | protein | 7 | — | — |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · 4 copies · chains A, B, C, D
- CL · Chloride ion · ion · 2 copies · chains B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5LVP · Human PDK1 Kinase Domain in Complex with an HM-Peptide Bound to the PIF-Pocket · the same entry in another collection · chain A against A, TM-score 1.00
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 O15530
- Elsewhere: RCSB PDB 5LVP · PDBe 5LVP · UniProt O15530
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.