Research workbench
Methionyl-tRNA synthetase zinc binding domain. 3D structure and homology with rubredoxin and gag retroviral proteins
Analyse Methionyl-tRNA synthetase zinc binding domain. 3D structure and homology with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1MED
- Type
- protein
- Length
- 28 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Methionyl-tRNA synthetase
- EC
- 6.1.1.10
- UniProt
- P00959
- Ligands
- ZN
Structure
solution nmr · 1 distinct chain · 0% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Methionyl-tRNA synthetase (EC 6.1.1.10) | protein | 28 | 0% helix, 7% strand | P00959 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1MED · Methionyl-tRNA synthetase zinc binding domain. 3D structure and homology with rubredoxin… · the same entry in another collection · chain A against A, TM-score 1.00
- P00959 · AlphaFold monomer V2.0 prediction for methionine--tRNA ligase (P00959) · a predicted model of the same protein · chain A against A, TM-score 0.25
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 P00959
- Elsewhere: RCSB PDB 1MED · PDBe 1MED · UniProt P00959
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