Research workbench
Crystallographic study of the complex of NI(II) schiff base complex and hew lysozyme
Analyse Crystallographic study of the complex of NI(II) schiff base complex and hew… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4KXI
- Type
- protein
- Length
- 129 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lysozyme C
- EC
- 3.2.1.17
- UniProt
- P00698
- Ligands
- LCP, SNF, NI, CL
- Pockets
- 1 · best druggability 0.34
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lysozyme C (EC 3.2.1.17) | protein | 129 | 42% helix, 11% strand | P00698 |
Ligands and binding sites
- LCP · Perchlorate ion · ligand · 5 copies · chains A
- SNF · (N1E, N2E)-N1, N2-bis(pyridine-2-ylmethylene)propane-1,2-diamine, nickel(II) salt · ligand · chains A
- NI · Nickel (II) ion · metal · chains A
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 69 | 0.34 | 0.76 | 18 | SNF |
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 4KXI · Crystallographic study of the complex of Ni(II) Schiff base complex and HEW Lysozyme · 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 P00698
- Elsewhere: RCSB PDB 4KXI · PDBe 4KXI · UniProt P00698
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