MolNFT v2 · #154318 · protein
Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 1 in complex with a piperidine-thienopyridine derivative
6JAV: “Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 1 in complex with a…”. X-ray diffraction at 1.437, 2 ligands (BC0, NAG). MolNFT v2 #154318 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6JAV
- Type
- protein
- Length
- 377 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.437
- Source
- Ostrinia furnacalis
- UniProt
- A0A221ZS22
- Ligands
- BC0, NAG
Structure
x-ray diffraction · resolution 1.437 · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 377 | — | A0A221ZS22 |
Ligands and binding sites
- BC0 · 2-{[(4-chlorophenyl)methyl]sulfanyl}-7-methyl-N-(prop-2-en-1-yl)-7,8-dihydropyrido[4',3':4,5]thieno[2,3-d]pyrimidin-4-amine · ligand · chains A
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6JAV · Crystal structure of ostrinia furnacalis group II chitinase catalytic domain 1 in complex… · 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 A0A221ZS22
- Elsewhere: RCSB PDB 6JAV · PDBe 6JAV · UniProt A0A221ZS22
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