MolNFT v1 · #91144 · protein
Conversion of the enzyme guanylate kinase into a mitotic spindle orienting protein by a single mutation that inhibits gmp- induced closing
4F4J: “Conversion of the enzyme guanylate kinase into a mitotic spindle orienting protein by a single mutation that…”. X-ray diffraction, 1 ligand (SO4), 3 pockets (best druggability 0.61). MolNFT v1 #91144 on GenesisL1: 3D structure…
- PDB
- 4F4J
- Type
- protein
- Length
- 375 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Guanylate kinase
- EC
- 2.7.4.8
- UniProt
- P15454
- Ligands
- SO4
- Pockets
- 3 · best druggability 0.61
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Guanylate kinase (EC 2.7.4.8) | protein | 189 | 43% helix, 21% strand | P15454 |
| B | Guanylate kinase (EC 2.7.4.8) | protein | 186 | 35% helix, 23% strand | P15454 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 5 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 479 | 0.61 | 0.75 | 44 | empty |
| 2 | 265 | 0.52 | 0.75 | 33 | SO4 |
| 3 | 123 | 0.40 | 0.75 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 742 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 4F4J · Conversion of the enzyme guanylate kinase into a mitotic spindle orienting protein by a… · the same entry in another collection · chain A against A, TM-score 1.00
- P15454 · AlphaFold monomer V2.0 prediction for guanylate kinase (P15454) · a predicted model of the same protein · chain A against A, TM-score 0.91
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 P15454
- Elsewhere: RCSB PDB 4F4J · PDBe 4F4J · UniProt P15454
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