MolNFT v2 · #10479 · protein
Crystal Structure Analysis of BST-1/CD157 complexed with ethenoNADP
1ISH: “Crystal Structure Analysis of BST-1/CD157 complexed with ethenoNADP”. X-ray diffraction at 2.4. MolNFT v2 #10479 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1ISH
- Type
- protein
- Length
- 500 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.4
- Source
- Homo sapiens
- UniProt
- Q10588
Structure
x-ray diffraction · resolution 2.4 · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 250 | — | Q10588 |
Compared structures
- 1ISH · Crystal structure analysis of bst-1/CD157 complexed with ethenonadp · the same entry in another collection · chain A against A, TM-score 1.00
- Q10588 · AlphaFold monomer V2.0 prediction for ADP-ribosyl CYCLASE/CYCLIC ADP- ribose hydrolase 2… · a predicted model of the same protein · 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 Q10588
- Elsewhere: RCSB PDB 1ISH · PDBe 1ISH · UniProt Q10588
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