MolNFT v1 · #187470 · protein
Mycobacterium tuberculosis HIP1 crystal structure
7SFM: “Mycobacterium tuberculosis HIP1 crystal structure”. X-ray diffraction, 4 pockets (best druggability 0.83). MolNFT v1 #187470 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7SFM
- Type
- protein
- Length
- 472 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- HIP1
- EC
- 3.4.-.-, 3.4.14.-
- UniProt
- A0A654TLU9
- Pockets
- 4 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | HIP1 (EC 3.4.-.-, 3.4.14.-) | protein | 472 | 45% helix, 14% strand | A0A654TLU9 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 775 | 0.83 | 0.86 | 88 | GOL, ACT |
| 2 | 118 | 0.58 | 0.85 | 17 | GOL |
| 3 | 68 | 0.48 | 0.84 | 18 | empty |
| 4 | 65 | 0.30 | 0.73 | 14 | empty |
Modifications
Observed in the structure: 6 modified, 5 disulfide (engineered, disulfide).
Compared structures
- 7SFM · Mycobacterium tuberculosis Hip1 crystal structure · 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 A0A654TLU9
- Elsewhere: RCSB PDB 7SFM · PDBe 7SFM · UniProt A0A654TLU9
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