MolNFT v1 · #20649 · protein
Crystal structure of creatine-ADP arginine kinase ternary complex
1RL9: “Crystal structure of creatine-ADP arginine kinase ternary complex”. X-ray diffraction, 3 ligands (ADP, IOM, MG), 1 pocket (best druggability 0.78). MolNFT v1 #20649 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1RL9
- Type
- protein
- Length
- 356 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Arginine kinase
- EC
- 2.7.3.3
- UniProt
- P51541
- Ligands
- ADP, IOM, MG
- Pockets
- 1 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Arginine kinase (EC 2.7.3.3) | protein | 356 | 39% helix, 17% strand | P51541 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · chains A
- IOM · (diaminomethyl-methyl-amino)-acetic acid · ligand · chains A
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 589 | 0.78 | 0.84 | 68 | MG, ADP, IOM |
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 P51541
- Elsewhere: RCSB PDB 1RL9 · PDBe 1RL9 · UniProt P51541
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