Research workbench
Crystal structure of 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase (ispf) from E. COLI involved in mevalonate-independent isoprenoid biosynthesis
Analyse Crystal structure of 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1KNK
- Type
- protein
- Length
- 156 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
- UniProt
- P62617
- Ligands
- MN
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase | protein | 156 | 27% helix, 26% strand | P62617 |
Ligands and binding sites
- MN · Manganese (II) ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1KNK · Crystal Structure of 2-C-methyl-D-erythritol 2,4-cyclodiphosphate Synthase (ispF) from E.… · the same entry in another collection · chain A against A, TM-score 1.00
- P62617 · AlphaFold monomer V2.0 prediction for 2-C-methyl-D-erythritol 2,4-cyclodiphosphate… · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P62617
- Elsewhere: RCSB PDB 1KNK · PDBe 1KNK · UniProt P62617
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