Research workbench
Crystal structures of FADD32 from corynebacterium diphtheriae
Analyse Crystal structures of FADD32 from corynebacterium diphtheriae in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7WUA
- Type
- protein
- Length
- 2,283 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A679LZK7
- Ligands
- ANP, MYR, MG
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 603 | — | A0A679LZK7 |
| B | — | protein | 597 | — | A0A679LZK7 |
| C | — | protein | 593 | — | A0A679LZK7 |
| D | — | protein | 490 | — | A0A679LZK7 |
Ligands and binding sites
- ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · 4 copies · chains A, B, C, D
- MYR · Myristic acid · ligand · 4 copies · chains A, B, C, D
- MG · Magnesium ion · metal · 2 copies · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7WUA · Crystal structures of FadD32 from Corynebacterium diphtheriae · 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 A0A679LZK7
- Elsewhere: RCSB PDB 7WUA · PDBe 7WUA · UniProt A0A679LZK7
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