MolNFT v1 · #14182 · protein
Transition state structure of arginine kinase
1M15: “Transition state structure of arginine kinase”. X-ray diffraction, 4 ligands (ARG, ADP, MG), 1 pocket (best druggability 0.76). MolNFT v1 #14182 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1M15
- 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
- ARG, ADP, MG, NO3
- Pockets
- 1 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Arginine kinase (EC 2.7.3.3) | protein | 356 | 41% helix, 18% strand | P51541 |
Ligands and binding sites
- ARG · Arginine · ligand · chains A
- ADP · Adenosine-5'-diphosphate · ligand · chains A
- MG · Magnesium ion · metal · chains A
- NO3 · Nitrate ion · ion · 2 copies · 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 | 481 | 0.76 | 0.85 | 63 | NO3, MG, ARG, ADP |
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 1M15 · PDBe 1M15 · UniProt P51541
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