Research workbench
Identification of amino acids that account for long-range interactions in proteins using two triosephosphate isomerases from pathogenic trypanosomes.
Analyse Identification of amino acids that account for long-range interactions in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3Q37
- Type
- protein
- Length
- 981 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P04789, P52270
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 242 | — | P04789, P52270 |
| B | — | protein | 243 | — | P04789, P52270 |
| C | — | protein | 248 | — | P04789, P52270 |
| D | — | protein | 248 | — | P04789, P52270 |
Compared structures
- 3Q37 · Identification of Amino Acids that Account for Long-Range Interactions in Proteins Using… · the same entry in another collection · chain C against C, 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 0.99
- P52270 · AlphaFold monomer V2.0 prediction for triosephosphate isomerase, glycosomal (P52270) · a predicted model of the same protein · chain B against A, TM-score 0.99
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
- Every structure of UniProt P52270
- Elsewhere: RCSB PDB 3Q37 · PDBe 3Q37 · UniProt P04789 · UniProt P52270
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