Research workbench
Crystal structure of triosephosphate isomerase from methicillin resistant staphylococcus aureus at 1.9 ångström resolution
Analyse Crystal structure of triosephosphate isomerase from methicillin resistant… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3M9Y
- Type
- protein
- Length
- 506 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Triosephosphate isomerase
- EC
- 5.3.1.1
- UniProt
- Q6GIL6
- Ligands
- NA
- Pockets
- 3 · best druggability 0.71
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Triosephosphate isomerase (EC 5.3.1.1) | protein | 252 | 46% helix, 15% strand | Q6GIL6 |
| B | Triosephosphate isomerase (EC 5.3.1.1) | protein | 254 | 44% helix, 15% strand | Q6GIL6 |
Ligands and binding sites
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 | 68 | 0.71 | 0.97 | 29 | NA |
| 2 | 104 | 0.44 | 0.79 | 28 | empty |
| 3 | 143 | 0.44 | 0.76 | 35 | CIT |
Interfaces
1 interface between chains.
- A–B · 1698 Ų buried · 20 hydrogen bonds · protein-protein
Compared structures
- 3M9Y · Crystal structure of Triosephosphate isomerase from methicillin resistant Staphylococcus… · the same entry in another collection · chain A against A, TM-score 1.00
- Q6GIL6 · AlphaFold monomer V2.0 prediction for triosephosphate isomerase (Q6GIL6) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q6GIL6
- Elsewhere: RCSB PDB 3M9Y · PDBe 3M9Y · UniProt Q6GIL6
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