Research workbench
Zymogen hgf-BETA/MET with zymogen activator peptide ZAP.14
Analyse Zymogen hgf-BETA/MET with zymogen activator peptide ZAP.14 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4O3T
- Type
- protein
- Length
- 727 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hepatocyte growth factor; Hepatocyte growth factor receptor; ZAP.14
- EC
- 2.7.10.1
- UniProt
- P14210, P08581
- Ligands
- NAG, FUC
- Pockets
- 8 · best druggability 0.72
Structure
x-ray diffraction · 3 distinct chains · 8% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hepatocyte growth factor | protein | 219 | 10% helix, 37% strand | P14210 |
| B | Hepatocyte growth factor receptor (EC 2.7.10.1) | protein | 499 | 7% helix, 44% strand | P08581 |
| P | ZAP.14 | protein | 9 | 0% helix, 33% strand | — |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains B
- FUC · alpha-L-fucopyranose · sugar
- 1PE · Pentaethylene glycol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 76 | 0.72 | 0.96 | 27 | empty |
| 2 | 694 | 0.71 | 0.78 | 52 | empty |
| 3 | 800 | 0.69 | 0.76 | 58 | empty |
| 4 | 167 | 0.56 | 0.81 | 31 | empty |
| 5 | 258 | 0.56 | 0.77 | 37 | empty |
Interfaces
2 interfaces between chains.
- A–B · 987 Ų buried · 20 hydrogen bonds · protein-protein
- A–P · 661 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 14 disulfide, 1 glycan (disulfide, N-glycosylation).
Compared structures
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 P14210
- Every structure of UniProt P08581
- Elsewhere: RCSB PDB 4O3T · PDBe 4O3T · UniProt P14210 · UniProt P08581
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