MolNFT v1 · #23954 · protein
Crystal analysis of chorismate mutase from thermus thermophilus
1UFY: “Crystal analysis of chorismate mutase from thermus thermophilus”. X-ray diffraction, 1 ligand (CL). MolNFT v1 #23954 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1UFY
- Type
- protein
- Length
- 121 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chorismate mutase
- EC
- 5.4.99.5
- UniProt
- Q84FH6
- Ligands
- CL
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chorismate mutase (EC 5.4.99.5) | protein | 121 | 36% helix, 28% strand | Q84FH6 |
Ligands and binding sites
- CL · Chloride ion · ion · chains A
- MES · 2-(N-morpholino)-ethanesulfonic acid · additive · 4 copies · chains A
- MLI · Malonate ion · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 Q84FH6
- Elsewhere: RCSB PDB 1UFY · PDBe 1UFY · UniProt Q84FH6
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