MolNFT v2 · #180041 · protein
Crystal structure of C-terminal half of lactoferrin obtained by limited proteolysis using pepsin at 2.6 A resolution
7EVQ: “Crystal structure of C-terminal half of lactoferrin obtained by limited proteolysis using pepsin at 2.6 A…”. X-ray diffraction at 2.6, 4 ligands (BCT, NAG, BMA). MolNFT v2 #180041 on GenesisL1: 3D structure, binding sites and…
- PDB
- 7EVQ
- Type
- protein
- Length
- 696 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.6
- Source
- Bos taurus
- UniProt
- P24627
- Ligands
- BCT, NAG, BMA, FE
Structure
x-ray diffraction · resolution 2.6 · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 348 | — | P24627 |
Ligands and binding sites
- BCT · Bicarbonate ion · ligand · 2 copies · chains A, B
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 10 copies · chains A, B
- BMA · beta-D-mannopyranose · sugar · 4 copies · chains B
- FE · Fe (III) ion · metal · 2 copies · chains A, B
- EDO · 1,2-ethanediol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7EVQ · Crystal structure of C-terminal half of lactoferrin obtained by limited proteolysis using… · 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 P24627
- Elsewhere: RCSB PDB 7EVQ · PDBe 7EVQ · UniProt P24627
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