MolNFT v1 · #51675 · protein
Structure-based enzyme engineering efforts with an inactive monomeric tim variant: the importance of a single point mutation for generating an active site with suitable binding properties
2VEL: “Structure-based enzyme engineering efforts with an inactive monomeric tim variant: the importance of a single…”. X-ray diffraction. MolNFT v1 #51675 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2VEL
- Type
- protein
- Length
- 476 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P04789
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 238 | — | P04789 |
Compared structures
- 2VEL · Structure-based enzyme engineering efforts with an inactive monomeric TIM variant: the… · the same entry in another collection · chain A against A, TM-score 1.00
- P04789 · AlphaFold monomer V2.0 prediction for triosephosphate isomerase, glycosomal (P04789) · a predicted model of the same protein · chain A against A, TM-score 0.97
- 4TIM · Crystallographic and molecular modeling studies on trypanosomal triosephosphate… · a predicted model of the same protein · chain A against A, TM-score 0.95
- 4TIM · Crystallographic and molecular modeling studies on trypanosomal triosephosphate… · a predicted model of the same protein · chain A against A, TM-score 0.95
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 2VEL · PDBe 2VEL · UniProt P04789
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