Research workbench
Structure-function studies on role of hydrophobic clamping of a basic glutamate in catalysis by triosephosphate isomerase
Analyse Structure-function studies on role of hydrophobic clamping of a basic glutamate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5I3G
- Type
- protein
- Length
- 996 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Triosephosphate isomerase, glycosomal
- EC
- 5.3.1.1
- UniProt
- P04789
- Pockets
- 7 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Triosephosphate isomerase, glycosomal (EC 5.3.1.1) | protein | 249 | 46% helix, 16% strand | P04789 |
Pockets
7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 718 | 0.77 | 0.82 | 85 | empty |
| 2 | 283 | 0.58 | 0.78 | 46 | empty |
| 3 | 232 | 0.53 | 0.77 | 31 | empty |
| 4 | 170 | 0.53 | 0.79 | 50 | empty |
| 5 | 129 | 0.51 | 0.80 | 37 | empty |
Interfaces
5 interfaces between chains.
- B–D · 1575 Ų buried · 31 hydrogen bonds · protein-protein
- A–C · 1566 Ų buried · 30 hydrogen bonds · protein-protein
- A–D · 334 Ų buried · 3 hydrogen bonds · protein-protein
- A–B · 153 Ų buried · 2 hydrogen bonds · protein-protein
- C–D · 70 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 5I3G · Structure-Function Studies on Role of Hydrophobic Clamping of a Basic Glutamate in… · the same entry in another collection · chain B against B, TM-score 1.00
- 4TIM · Crystallographic and molecular modeling studies on trypanosomal triosephosphate… · a predicted model of the same protein · chain B against A, TM-score 1.00
- 4TIM · Crystallographic and molecular modeling studies on trypanosomal triosephosphate… · a predicted model of the same protein · chain B 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 P04789
- Elsewhere: RCSB PDB 5I3G · PDBe 5I3G · UniProt P04789
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