Research workbench
Structure of HGH1, crystal form I
Analyse Structure of HGH1, crystal form I in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6HB1
- Type
- protein
- Length
- 1,429 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein HGH1
- UniProt
- P48362
- Ligands
- CL
- Pockets
- 18 · best druggability 0.60
Structure
x-ray diffraction · 4 distinct chains · 64% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein HGH1 | protein | 357 | 63% helix, 2% strand | P48362 |
| B | Protein HGH1 | protein | 357 | 64% helix, 3% strand | P48362 |
| C | Protein HGH1 | protein | 356 | 64% helix, 3% strand | P48362 |
| D | Protein HGH1 | protein | 359 | 64% helix, 3% strand | P48362 |
Ligands and binding sites
- CL · Chloride ion · ion · 3 copies · chains A, D, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
18 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 351 | 0.60 | 0.77 | 38 | CL |
| 2 | 300 | 0.57 | 0.76 | 28 | CL |
| 3 | 281 | 0.55 | 0.76 | 43 | empty |
| 4 | 148 | 0.47 | 0.78 | 31 | empty |
| 5 | 115 | 0.47 | 0.79 | 17 | empty |
Interfaces
4 interfaces between chains.
- C–D · 664 Ų buried · 6 hydrogen bonds · protein-protein
- A–B · 592 Ų buried · 9 hydrogen bonds · protein-protein
- B–C · 560 Ų buried · 5 hydrogen bonds · protein-protein
- A–D · 543 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- P48362 · AlphaFold monomer V2.0 prediction for protein HGH1 (P48362) · a predicted model of the same protein · chain C 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 P48362
- Elsewhere: RCSB PDB 6HB1 · PDBe 6HB1 · UniProt P48362
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