MolNFT v2 · #152495 · protein
Structure of EAL Enzyme Bd1971 - halfsite-occupied form
6HQ3: “Structure of EAL Enzyme Bd1971 - halfsite-occupied form”. X-ray diffraction at 2.79, 1 ligand (CMP). MolNFT v2 #152495 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6HQ3
- Type
- protein
- Length
- 434 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.79
- Source
- Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIB 9529 / HD100)
- UniProt
- Q6MLN6
- Ligands
- CMP
Structure
x-ray diffraction · resolution 2.79 · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 111 | — | Q6MLN6 |
| B, D | — | protein | 107 | — | Q6MLN6 |
| C | — | protein | 109 | — | Q6MLN6 |
Ligands and binding sites
- CMP · Adenosine-3',5'-cyclic-monophosphate · ligand · 2 copies · chains B, C, A, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6HQ3 · Structure of eal enzyme BD1971 - halfsite-occupied form · 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 Q6MLN6
- Elsewhere: RCSB PDB 6HQ3 · PDBe 6HQ3 · UniProt Q6MLN6
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