MolNFT v1 · #3195 · protein
Cmp kinase from escherichia COLI free enzyme structure
1CKE · Protein (cytidine monophosphate kinase): “Cmp kinase from escherichia COLI free enzyme structure”. X-ray diffraction, 1 ligand (SO4), 2 pockets (best druggability 0.62). MolNFT v1 #3195 on GenesisL1: 3D structure, binding sites and…
- PDB
- 1CKE
- Type
- protein
- Length
- 212 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (cytidine monophosphate kinase)
- EC
- 2.7.4.14
- UniProt
- P0A6I0
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (cytidine monophosphate kinase) (EC 2.7.4.14) | protein | 212 | 50% helix, 18% strand | P0A6I0 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 564 | 0.62 | 0.75 | 48 | SO4 |
| 2 | 50 | 0.26 | 0.74 | 16 | empty |
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 P0A6I0
- Elsewhere: RCSB PDB 1CKE · PDBe 1CKE · UniProt P0A6I0
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