MolNFT v1 · #47777 · protein
AlphaFold monomer V2.0 prediction for complement C1S subcomponent (P09871)
P09871: “AlphaFold monomer V2.0 prediction for complement C1S subcomponent (P09871)”. MolNFT v1 #47777 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- P09871
- Type
- protein
- Length
- 688 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6F96E7ECD556d5E02BecEf6eBE49253734162c59
- UniProt
- P09871
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 688 | — | P09871 |
Compared structures
- 4J1Y · The X-ray crystal structure of human complement protease C1S zymogen · an experimental structure of the same protein · chain A against A, TM-score 0.53
- 4J1Y · The X-ray crystal structure of human complement protease C1s zymogen · an experimental structure of the same protein · chain A against A, TM-score 0.53
- 8TYP · Complement Protease C1s Inhibited by 6-(4-phenylpiperazin-1-yl)pyridine-3-carboximidamide · an experimental structure of the same protein · chain A against A, TM-score 0.44
- 1ELV · Crystal structure of the catalytic domain of human complement C1S protease · an experimental structure of the same protein · chain A against A, TM-score 0.44
- 1ELV · Crystal structure of the catalytic domain of human complement C1S protease · an experimental structure of the same protein · chain A against A, TM-score 0.44
- 8GMN · Crystal structure of human C1s in complex with inhibitor · an experimental structure of the same protein · chain A against A, TM-score 0.40
- 4LMF · C1s CUB1-EGF-CUB2 · an experimental structure of the same protein · chain A against B, TM-score 0.35
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 P09871
- Elsewhere: UniProt P09871 · AlphaFold DB P09871
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