MolNFT v1 · #100364 · protein
1.43 ångström resolution crystal structure of triosephosphate isomerase (tpia) from escherichia COLI in complex with acetyl phosphate.
4MVA: “1.43 ångström resolution crystal structure of triosephosphate isomerase (tpia) from escherichia COLI in…”. X-ray diffraction, 3 ligands (UVW, CL, PO4), 4 pockets (best druggability 0.66). MolNFT v1 #100364 on GenesisL1: 3D…
- 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
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