MolNFT v1 · #38896 · protein
Acidic residues at the active sites of CD38 and ADP-ribosyl cyclase determine naapd synthesis and hydrolysis activities
2HCT: “Acidic residues at the active sites of CD38 and ADP-ribosyl cyclase determine naapd synthesis and hydrolysis…”. X-ray diffraction. MolNFT v1 #38896 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2HCT
- Type
- protein
- Length
- 504 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P28907
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 252 | — | P28907 |
Compared structures
- 2HCT · Acidic residues at the active sites of CD38 and ADP-ribosyl cyclase determine NAAPD… · the same entry in another collection · chain B against B, TM-score 1.00
- P28907 · AlphaFold monomer V2.0 prediction for ADP-ribosyl CYCLASE/CYCLIC ADP- ribose hydrolase 1… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P28907
- Elsewhere: RCSB PDB 2HCT · PDBe 2HCT · UniProt P28907
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