Research workbench
Kinetic and structural changes in hsmtphers, induced by pathogenic mutations in human FARS2
Analyse Kinetic and structural changes in hsmtphers, induced by pathogenic mutations in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5MGU
- Type
- protein
- Length
- 408 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O95363
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 408 | — | O95363 |
Compared structures
- 5MGU · Kinetic and Structural Changes in HsmtPheRS, Induced by Pathogenic Mutations in Human… · the same entry in another collection · chain A against A, TM-score 1.00
- O95363 · AlphaFold monomer V2.0 prediction for phenylalanine--tRNA ligase, mitochondrial (O95363) · 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 O95363
- Elsewhere: RCSB PDB 5MGU · PDBe 5MGU · UniProt O95363
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