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Crystal structure of marh, an epimerase for biosynthesis of maremycins in streptomyces, under pH 4.7, without zn
Analyse Crystal structure of marh, an epimerase for biosynthesis of maremycins in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6J4D
- Type
- protein
- Length
- 122 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cupin superfamily protein
- UniProt
- X2D812
- Pockets
- 1 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 2% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cupin superfamily protein | protein | 122 | 2% helix, 44% strand | X2D812 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 136 | 0.66 | 0.88 | 28 | FLC |
Compared structures
- 6J4D · Crystal structure of MarH, an epimerase for biosynthesis of Maremycins in Streptomyces… · 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 X2D812
- Elsewhere: RCSB PDB 6J4D · PDBe 6J4D · UniProt X2D812
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