MolNFT v1 · #29899 · protein
Catalytic and ubiqutin-associated domains of MARK2/PAR-1: K82R mutant
1ZMV · MAP/MICROTUBULE affinity regulating kinase 2: “Catalytic and ubiqutin-associated domains of MARK2/PAR-1: K82R mutant”. X-ray diffraction, 5 pockets (best druggability 0.71). MolNFT v1 #29899 on GenesisL1: 3D structure, binding sites…
- PDB
- 1ZMV
- Type
- protein
- Length
- 589 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- MAP/MICROTUBULE affinity regulating kinase 2
- EC
- 2.7.1.37
- UniProt
- O08679
- Pockets
- 5 · best druggability 0.71
Structure
x-ray diffraction · 2 distinct chains · 44% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | MAP/MICROTUBULE affinity regulating kinase 2 (EC 2.7.1.37) | protein | 293 | 44% helix, 15% strand | O08679 |
| B | MAP/MICROTUBULE affinity regulating kinase 2 (EC 2.7.1.37) | protein | 296 | 44% helix, 15% strand | O08679 |
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 661 | 0.71 | 0.78 | 51 | empty |
| 2 | 630 | 0.70 | 0.78 | 50 | empty |
| 3 | 237 | 0.52 | 0.76 | 28 | empty |
| 4 | 204 | 0.50 | 0.76 | 27 | empty |
| 5 | 54 | 0.31 | 0.76 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 922 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 1ZMV · Catalytic and ubiqutin-associated domains of MARK2/PAR-1: K82R mutant · the same entry in another collection · chain A against A, TM-score 1.00
- O08679 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein kinase MARK2 (O08679) · a predicted model of the same protein · chain B against A, TM-score 0.98
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 O08679
- Elsewhere: RCSB PDB 1ZMV · PDBe 1ZMV · UniProt O08679
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