MolNFT v1 · #148209 · protein
Crystal structure of human glycosylated kallistatin at 3.0 ångström resolution
6F02: “Crystal structure of human glycosylated kallistatin at 3.0 ångström resolution”. X-ray diffraction, 4 ligands (NAG, FUL, BMA). MolNFT v1 #148209 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6F02
- Type
- protein
- Length
- 745 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P29622
- Ligands
- NAG, FUL, BMA, SO4
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 370 | — | P29622 |
| C | — | protein | 375 | — | P29622 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 7 copies · chains A, C
- FUL · beta-L-fucopyranose · sugar · 4 copies · chains A, C
- BMA · beta-D-mannopyranose · sugar · 3 copies · chains C, A
- SO4 · Sulfate ion · ion · 2 copies · chains C, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6F02 · Crystal structure of human glycosylated kallistatin at 3.0 Angstrom resolution · the same entry in another collection · chain A against A, TM-score 1.00
- P29622 · AlphaFold monomer V2.0 prediction for kallistatin (P29622) · a predicted model of the same protein · 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 P29622
- Elsewhere: RCSB PDB 6F02 · PDBe 6F02 · UniProt P29622
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