MolNFT v1 · #90538 · protein
Crystal structure of ispe (4-diphosphocytidyl-2-C-methyl-D-erythritol kinase) from mycobacterium abcessus, bound to cmp and SO4
4EMD: “Crystal structure of ispe (4-diphosphocytidyl-2-C-methyl-D-erythritol kinase) from mycobacterium abcessus…”. X-ray diffraction, 2 ligands (C5P, SO4), 1 pocket (best druggability 0.65). MolNFT v1 #90538 on GenesisL1: 3D structure…
- PDB
- 4EMD
- Type
- protein
- Length
- 299 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase
- EC
- 2.7.1.148
- UniProt
- B1MKD5
- Ligands
- C5P, SO4
- Pockets
- 1 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase (EC 2.7.1.148) | protein | 299 | 35% helix, 31% strand | B1MKD5 |
Ligands and binding sites
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 | 369 | 0.65 | 0.79 | 43 | C5P, SO4 |
Compared structures
- 4EMD · Crystal structure of IspE (4-diphosphocytidyl-2-C-methyl-D-erythritol kinase) from… · 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 B1MKD5
- Elsewhere: RCSB PDB 4EMD · PDBe 4EMD · UniProt B1MKD5
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