Research workbench
Human triosephosphate isomerase mutant V231M
Analyse Human triosephosphate isomerase mutant V231M in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6C2G
- Type
- protein
- Length
- 972 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.3
- Source
- Homo sapiens
- Molecule
- Triosephosphate isomerase
- EC
- 5.3.1.1
- UniProt
- P60174
- Pockets
- 9 · best druggability 0.74
Structure
x-ray diffraction · resolution 2.3 · 3 distinct chains · 44% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Triosephosphate isomerase (EC 5.3.1.1) | protein | 244 | 45% helix, 16% strand | P60174 |
| C | Triosephosphate isomerase (EC 5.3.1.1) | protein | 243 | 45% helix, 16% strand | P60174 |
| D | Triosephosphate isomerase (EC 5.3.1.1) | protein | 241 | 42% helix, 17% strand | P60174 |
Pockets
9 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 830 | 0.74 | 0.78 | 74 | empty |
| 2 | 56 | 0.67 | 0.96 | 16 | empty |
| 3 | 146 | 0.49 | 0.78 | 20 | empty |
| 4 | 88 | 0.39 | 0.77 | 18 | empty |
| 5 | 94 | 0.38 | 0.76 | 21 | empty |
Interfaces
3 interfaces between chains.
- B–D · 1775 Ų buried · 40 hydrogen bonds · protein-protein
- A–B · 431 Ų buried · 5 hydrogen bonds · protein-protein
- B–C · 222 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
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 P60174
- Elsewhere: RCSB PDB 6C2G · PDBe 6C2G · UniProt P60174
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