MolNFT v1 · #55034 · protein
Structure of human phosphorylase kinase, gamma 2
2Y7J · Phosphorylase B kinase gamma catalytic chain, TESTIS/LIVER…: “Structure of human phosphorylase kinase, gamma 2”. X-ray diffraction, 1 ligand (B49), 11 pockets (best druggability 0.75). MolNFT v1 #55034 on GenesisL1: 3D structure…
- PDB
- 2Y7J
- Type
- protein
- Length
- 1,130 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphorylase B kinase gamma catalytic chain, TESTIS/LIVER isoform
- EC
- 2.7.11.19
- UniProt
- P15735
- Ligands
- B49
- Pockets
- 11 · best druggability 0.75
Structure
x-ray diffraction · 3 distinct chains · 43% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Phosphorylase B kinase gamma catalytic chain, TESTIS/LIVER isoform (EC 2.7.11.19) | protein | 284 | 42% helix, 19% strand | P15735 |
| B | Phosphorylase B kinase gamma catalytic chain, TESTIS/LIVER isoform (EC 2.7.11.19) | protein | 281 | 43% helix, 19% strand | P15735 |
| D | Phosphorylase B kinase gamma catalytic chain, TESTIS/LIVER isoform (EC 2.7.11.19) | protein | 281 | 42% helix, 20% strand | P15735 |
Ligands and binding sites
- B49 · N-[2-(diethylamino)ethyl]-5-[(Z)-(5-fluoro-2-oxo-1,2-dihydro-3H-indol-3-ylidene)methyl]-2,4-dimethyl-1H-pyrrole-3-carboxamide · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 230 | 0.75 | 0.89 | 29 | empty |
| 2 | 303 | 0.71 | 0.85 | 31 | empty |
| 3 | 468 | 0.68 | 0.79 | 54 | B49 |
| 4 | 511 | 0.67 | 0.78 | 54 | B49 |
| 5 | 443 | 0.66 | 0.79 | 42 | B49 |
Interfaces
4 interfaces between chains.
- A–C · 839 Ų buried · 7 hydrogen bonds · protein-protein
- B–C · 760 Ų buried · 9 hydrogen bonds · protein-protein
- A–D · 701 Ų buried · 11 hydrogen bonds · protein-protein
- B–D · 674 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
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 P15735
- Elsewhere: RCSB PDB 2Y7J · PDBe 2Y7J · UniProt P15735
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.