Research workbench
1.43 ångström resolution crystal structure of triosephosphate isomerase (tpia) from escherichia COLI in complex with acetyl phosphate.
Analyse 1.43 ångström resolution crystal structure of triosephosphate isomerase (tpia)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4MVA
- Type
- protein
- Length
- 509 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Triosephosphate isomerase
- EC
- 5.3.1.1
- UniProt
- C5A086
- Ligands
- UVW, CL, PO4
- Pockets
- 4 · best druggability 0.66
Structure
x-ray diffraction · 2 distinct chains · 49% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Triosephosphate isomerase (EC 5.3.1.1) | protein | 255 | 49% helix, 15% strand | C5A086 |
| B | Triosephosphate isomerase (EC 5.3.1.1) | protein | 254 | 49% helix, 16% strand | C5A086 |
Ligands and binding sites
- UVW · Acetylphosphate · ligand · 2 copies · chains A, B
- CL · Chloride ion · ion · chains A
- PO4 · Phosphate ion · ion · chains A, B
- EDO · 1,2-ethanediol · additive · 2 copies · chains A, B
- PEG · Di(hydroxyethyl)ether · additive · chains B
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 | 287 | 0.66 | 0.82 | 44 | empty |
| 2 | 192 | 0.53 | 0.78 | 28 | UVW, PEG |
| 3 | 91 | 0.42 | 0.79 | 25 | UVW |
| 4 | 54 | 0.29 | 0.76 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 1681 Ų buried · 32 hydrogen bonds · protein-protein
Compared structures
- 4MVA · 1.43 Angstrom Resolution Crystal Structure of Triosephosphate Isomerase (tpiA) from… · 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 C5A086
- Elsewhere: RCSB PDB 4MVA · PDBe 4MVA · UniProt C5A086
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.