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Moac protein from E. COLI
Analyse Moac protein from E. COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1EKR
- Type
- protein
- Length
- 143 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Molybdenum cofactor biosynthesis protein C
- UniProt
- P0A738
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Molybdenum cofactor biosynthesis protein C | protein | 143 | 36% helix, 31% strand | P0A738 |
Compared structures
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 P0A738
- Elsewhere: RCSB PDB 1EKR · PDBe 1EKR · UniProt P0A738
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