MolNFT v1 · #151022 · protein
Structure of HGH1, crystal form I, selenomethionine derivative
6HB2 · Protein HGH1: “Structure of HGH1, crystal form I, selenomethionine derivative”. X-ray diffraction, 1 ligand (CL), 17 pockets (best druggability 0.74). MolNFT v1 #151022 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6HB2
- Type
- protein
- Length
- 1,428 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein HGH1
- UniProt
- P48362
- Ligands
- CL
- Pockets
- 17 · best druggability 0.74
Structure
x-ray diffraction · 4 distinct chains · 64% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein HGH1 | protein | 354 | 63% helix, 2% strand | P48362 |
| B | Protein HGH1 | protein | 359 | 64% helix, 2% strand | P48362 |
| C | Protein HGH1 | protein | 357 | 64% helix, 2% strand | P48362 |
| D | Protein HGH1 | protein | 358 | 65% helix, 2% strand | P48362 |
Ligands and binding sites
- CL · Chloride ion · ion · chains D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
17 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 65 | 0.74 | 0.98 | 14 | empty |
| 2 | 339 | 0.62 | 0.79 | 43 | empty |
| 3 | 373 | 0.62 | 0.77 | 42 | empty |
| 4 | 277 | 0.57 | 0.77 | 30 | empty |
| 5 | 322 | 0.57 | 0.76 | 40 | empty |
Interfaces
4 interfaces between chains.
- C–D · 658 Ų buried · 8 hydrogen bonds · protein-protein
- A–B · 635 Ų buried · 5 hydrogen bonds · protein-protein
- B–C · 561 Ų buried · 4 hydrogen bonds · protein-protein
- A–D · 538 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 39 modified (engineered).
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 P48362
- Elsewhere: RCSB PDB 6HB2 · PDBe 6HB2 · UniProt P48362
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