MolNFT v1 · #40028 · protein
Crystal structure of hypothetical protein AF0160 from archaeoglobus fulgidus
2IDG: “Crystal structure of hypothetical protein AF0160 from archaeoglobus fulgidus”. X-ray diffraction, 4 pockets (best druggability 0.65). MolNFT v1 #40028 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2IDG
- Type
- protein
- Length
- 487 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical protein AF0160
- UniProt
- O30077
- Pockets
- 4 · best druggability 0.65
Structure
x-ray diffraction · 3 distinct chains · 69% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hypothetical protein AF0160 | protein | 160 | 69% helix, 1% strand | O30077 |
| B | Hypothetical protein AF0160 | protein | 163 | 70% helix, 1% strand | O30077 |
| C | Hypothetical protein AF0160 | protein | 164 | 70% helix, 1% strand | O30077 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 476 | 0.65 | 0.77 | 31 | empty |
| 2 | 224 | 0.53 | 0.76 | 26 | empty |
| 3 | 102 | 0.36 | 0.73 | 21 | empty |
| 4 | 99 | 0.35 | 0.74 | 25 | empty |
Interfaces
2 interfaces between chains.
- B–C · 656 Ų buried · 2 hydrogen bonds · protein-protein
- A–B · 399 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 15 modified (engineered).
Compared structures
- 2IDG · Crystal Structure of hypothetical protein AF0160 from Archaeoglobus fulgidus · the same entry in another collection · chain A against A, TM-score 1.00
- O30077 · AlphaFold monomer V2.0 prediction for tat proofreading chaperone ttrd (O30077) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 O30077
- Elsewhere: RCSB PDB 2IDG · PDBe 2IDG · UniProt O30077
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