Research workbench
Structure determination of the cancer-associated mycoplasma hyorhinis protein mh-P37
Analyse Structure determination of the cancer-associated mycoplasma hyorhinis protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3E79
- Type
- protein
- Length
- 365 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- High affinity transport system protein P37
- UniProt
- P15363
- Ligands
- I3C, TPP, CA, CL
- Pockets
- 3 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | High affinity transport system protein P37 | protein | 365 | 41% helix, 21% strand | P15363 |
Ligands and binding sites
- I3C · 5-amino-2,4,6-triiodobenzene-1,3-dicarboxylic acid · ligand · 2 copies · chains A
- TPP · Thiamine diphosphate · ligand · chains A
- CA · Calcium ion · metal · chains A
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 589 | 0.70 | 0.78 | 68 | TPP |
| 2 | 85 | 0.37 | 0.76 | 15 | empty |
| 3 | 57 | 0.32 | 0.76 | 14 | I3C |
Compared structures
- 3E79 · Structure determination of the cancer-associated Mycoplasma hyorhinis protein Mh-p37 · the same entry in another collection · chain A against A, TM-score 1.00
- P15363 · AlphaFold monomer V2.0 prediction for high affinity transport system protein P37 (P15363) · a predicted model of the same protein · 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 P15363
- Elsewhere: RCSB PDB 3E79 · PDBe 3E79 · UniProt P15363
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