MolNFT v1 · #69840 · protein
Glycocyamine kinase, alpha-beta heterodimer from marine worm namalycastis sp.
3L2E · Glycocyamine kinase alpha chain: “Glycocyamine kinase, alpha-beta heterodimer from marine worm namalycastis sp.”. X-ray diffraction, 18 pockets (best druggability 0.83). MolNFT v1 #69840 on GenesisL1: 3D structure, binding sites and…
- PDB
- 3L2E
- Type
- protein
- Length
- 1,509 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glycocyamine kinase alpha chain; Glycocyamine kinase beta chain
- EC
- 2.7.3.1
- UniProt
- Q6AW43, Q6AW42
- Pockets
- 18 · best druggability 0.83
Structure
x-ray diffraction · 3 distinct chains · 37% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Glycocyamine kinase alpha chain (EC 2.7.3.1) | protein | 373 | 37% helix, 18% strand | Q6AW43 |
| B | Glycocyamine kinase beta chain (EC 2.7.3.1) | protein | 383 | 37% helix, 17% strand | Q6AW42 |
| D | Glycocyamine kinase beta chain (EC 2.7.3.1) | protein | 380 | 38% helix, 16% strand | Q6AW42 |
Pockets
18 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 529 | 0.83 | 0.89 | 64 | empty |
| 2 | 434 | 0.83 | 0.91 | 64 | empty |
| 3 | 320 | 0.70 | 0.84 | 38 | empty |
| 4 | 592 | 0.66 | 0.76 | 72 | empty |
| 5 | 84 | 0.63 | 0.90 | 20 | empty |
Interfaces
4 interfaces between chains.
- A–B · 1659 Ų buried · 35 hydrogen bonds · protein-protein
- C–D · 1645 Ų buried · 29 hydrogen bonds · protein-protein
- A–D · 943 Ų buried · 6 hydrogen bonds · protein-protein
- A–C · 67 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 3L2E · Glycocyamine kinase, alpha-beta heterodimer from marine worm Namalycastis sp. · 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 Q6AW43
- Every structure of UniProt Q6AW42
- Elsewhere: RCSB PDB 3L2E · PDBe 3L2E · UniProt Q6AW43 · UniProt Q6AW42
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