MolNFT v1 · #178465 · protein
Chlorovirus pbcv-1 bi-functional DCMP/DCTP deaminase bi-dcd
7FH4: “Chlorovirus pbcv-1 bi-functional DCMP/DCTP deaminase bi-dcd”. X-ray diffraction, 4 ligands (DCM, DCP, ZN). MolNFT v1 #178465 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7FH4
- Type
- protein
- Length
- 280 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O41078
- Ligands
- DCM, DCP, ZN, MG
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 140 | — | O41078 |
Ligands and binding sites
- DCM · 2'-deoxycytidine-5'-monophosphate · ligand · 2 copies · chains A, B
- DCP · 2'-deoxycytidine-5'-triphosphate · ligand · 2 copies · chains A, B
- ZN · Zinc ion · metal · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7FH4 · Chlorovirus PBCV-1 bi-functional dCMP/dCTP deaminase bi-DCD · 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 O41078
- Elsewhere: RCSB PDB 7FH4 · PDBe 7FH4 · UniProt O41078
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