Research workbench
Mechanism of the reaction catalyzed by mandelate racemase. 2. crystal structure of mandelate racemase at 2.5 ångströms resolution: identification of the active site and possible catalytic residues
Analyse Mechanism of the reaction catalyzed by mandelate racemase. 2. crystal structure… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2MNR
- Type
- protein
- Length
- 357 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P11444
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 357 | — | P11444 |
Compared structures
- 2MNR · Mechanism of the reaction catalyzed by mandelate racemase. 2. crystal structure of… · the same entry in another collection · chain A against A, TM-score 1.00
- P11444 · AlphaFold monomer V2.0 prediction for mandelate racemase (P11444) · a predicted model of the same protein · chain A 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 P11444
- Elsewhere: RCSB PDB 2MNR · PDBe 2MNR · UniProt P11444
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.