MolNFT v1 · #38705 · protein
X-ray crystal structure of the metal-containing protein AF0104 from archaeoglobus fulgidus. northeast structural genomics consortium target GR103.
2H6L · Hypothetical protein: “X-ray crystal structure of the metal-containing protein AF0104 from archaeoglobus fulgidus. northeast…”. X-ray diffraction, 1 ligand (ZN), 3 pockets (best druggability 0.57). MolNFT v1 #38705 on GenesisL1: 3D…
- PDB
- 2H6L
- Type
- protein
- Length
- 420 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical protein
- UniProt
- O30132
- Ligands
- ZN
- Pockets
- 3 · best druggability 0.57
Structure
x-ray diffraction · 1 distinct chain · 9% helix, 66% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Hypothetical protein | protein | 140 | 9% helix, 66% strand | O30132 |
Ligands and binding sites
- ZN · Zinc ion · metal · 3 copies · chains A, C, B
- ACY · Acetic acid · additive · 3 copies · chains A, C, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 161 | 0.57 | 0.82 | 28 | ACY |
| 2 | 144 | 0.57 | 0.82 | 30 | ACY |
| 3 | 82 | 0.52 | 0.84 | 21 | ACY |
Interfaces
3 interfaces between chains.
- A–B · 1747 Ų buried · 24 hydrogen bonds · protein-protein
- B–C · 1745 Ų buried · 24 hydrogen bonds · protein-protein
- A–C · 1738 Ų buried · 24 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 9 modified (engineered).
Compared structures
- 2H6L · X-Ray Crystal Structure of the Metal-containing Protein AF0104 from Archaeoglobus… · 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 O30132
- Elsewhere: RCSB PDB 2H6L · PDBe 2H6L · UniProt O30132
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