Research workbench
Crystal structure of the regulatory domain of licms in complexed with isoleucine - type III
Analyse Crystal structure of the regulatory domain of licms in complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3F6H
- Type
- protein
- Length
- 244 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-isopropylmalate synthase
- EC
- 2.3.1.182
- UniProt
- Q8F3Q1
- Ligands
- ILE, ZN
Structure
x-ray diffraction · 2 distinct chains · 25% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-isopropylmalate synthase (EC 2.3.1.182) | protein | 119 | 26% helix, 43% strand | Q8F3Q1 |
| B | Alpha-isopropylmalate synthase (EC 2.3.1.182) | protein | 125 | 25% helix, 39% strand | Q8F3Q1 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 513 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 3F6H · Crystal structure of the regulatory domain of LiCMS in complexed with isoleucine - type… · the same entry in another collection · chain B against B, TM-score 1.00
- Q8F3Q1 · AlphaFold monomer V2.0 prediction for (R)-citramalate synthase cima (Q8F3Q1) · a predicted model of the same protein · chain B against A, TM-score 0.97
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 Q8F3Q1
- Elsewhere: RCSB PDB 3F6H · PDBe 3F6H · UniProt Q8F3Q1
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