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Crystal structure of C-as lyase with FE(III)
Analyse Crystal structure of C-as lyase with FE(III) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5D4F
- Type
- protein
- Length
- 108 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GLYOXALASE/BLEOMYCIN resistance PROTEIN/DIOXYGENASE
- UniProt
- D1A230
- Ligands
- NA, FE, CL
Structure
x-ray diffraction · 1 distinct chain · 23% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | GLYOXALASE/BLEOMYCIN resistance PROTEIN/DIOXYGENASE | protein | 108 | 23% helix, 44% strand | D1A230 |
Ligands and binding sites
- NA · Sodium ion · metal · 3 copies · chains A
- FE · Fe (III) ion · metal · chains A
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5D4F · Crystal structure of C-As lyase with Fe(III) · 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 D1A230
- Elsewhere: RCSB PDB 5D4F · PDBe 5D4F · UniProt D1A230
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