Research workbench
Structure of F420-H2 dependent reductase (fdr-a) MSMEG_2027
Analyse Structure of F420-H2 dependent reductase (fdr-a) MSMEG_2027 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4Y9I
- Type
- protein
- Length
- 114 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mycobacterium tuberculosis paralogous family 11
- UniProt
- A0QU01
- Ligands
- PO4
Structure
x-ray diffraction · 1 distinct chain · 25% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mycobacterium tuberculosis paralogous family 11 | protein | 114 | 25% helix, 36% strand | A0QU01 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 4Y9I · Structure of F420-H2 Dependent Reductase (FDR-A) msmeg_2027 · the same entry in another collection · chain A against A, TM-score 1.00
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 A0QU01
- Elsewhere: RCSB PDB 4Y9I · PDBe 4Y9I · UniProt A0QU01
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