MolNFT v1 · #53676 · protein
Crystallographic binding studies with an engineered monomeric variant of triosephosphate isomerase
2X1T: “Crystallographic binding studies with an engineered monomeric variant of triosephosphate isomerase”. X-ray diffraction. MolNFT v1 #53676 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2X1T
- Type
- protein
- Length
- 471 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P04789
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 233 | — | P04789 |
| B | — | protein | 238 | — | P04789 |
Compared structures
- 2X1T · Crystallographic binding studies with an engineered monomeric variant of triosephosphate… · the same entry in another collection · chain A against A, TM-score 1.00
- 4TIM · Crystallographic and molecular modeling studies on trypanosomal triosephosphate… · a predicted model of the same protein · chain A against A, TM-score 0.98
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 2X1T · PDBe 2X1T · UniProt P04789
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