Research workbench
Crystal structure of cleaved human ALPHA1-antichymotrypsin at 2.7 ångströms resolution and its comparison with other serpins
Analyse Crystal structure of cleaved human ALPHA1-antichymotrypsin at 2.7 ångströms… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ACH
- Type
- protein
- Length
- 372 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P01011
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 337 | — | P01011 |
| B | — | protein | 35 | — | P01011 |
Compared structures
- 2ACH · Crystal structure of cleaved human ALPHA1-antichymotrypsin at 2.7 ångströms resolution… · the same entry in another collection · chain A against A, TM-score 1.00
- P01011 · AlphaFold monomer V2.0 prediction for alpha-1-antichymotrypsin (P01011) · a predicted model of the same protein · chain A against A, TM-score 0.93
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 P01011
- Elsewhere: RCSB PDB 2ACH · PDBe 2ACH · UniProt P01011
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