Research workbench
Glycosilated human serum apo-tranferrin
Analyse Glycosilated human serum apo-tranferrin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7Q1L
- Type
- protein
- Length
- 1,352 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Serotransferrin
- UniProt
- P02787
- Ligands
- NAG, MG, SO4
- Pockets
- 12 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Serotransferrin | protein | 676 | 36% helix, 17% strand | P02787 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A, B
- MG · Magnesium ion · metal · chains A
- SO4 · Sulfate ion · ion · 2 copies · chains B
- GOL · Glycerol · additive · 7 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1016 | 0.77 | 0.79 | 72 | empty |
| 2 | 641 | 0.73 | 0.80 | 56 | empty |
| 3 | 679 | 0.68 | 0.76 | 68 | GOL, EDO |
| 4 | 558 | 0.66 | 0.77 | 46 | GOL, EDO |
| 5 | 504 | 0.62 | 0.75 | 45 | empty |
Interfaces
1 interface between chains.
- A–B · 1069 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 38 disulfide, 1 glycan (disulfide, N-glycosylation).
Compared structures
- 7Q1L · Glycosilated Human Serum Apo-tranferrin · 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 P02787
- Elsewhere: RCSB PDB 7Q1L · PDBe 7Q1L · UniProt P02787
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