MolNFT v1 · #177752 · protein
Interaction of the peptide CF3-leu-ala-nh-C6H4-CF3(TFLA) with porcine pancreatic elastase. X-ray studies at 1.8 ångströms
7EST: “Interaction of the peptide CF3-leu-ala-nh-C6H4-CF3(TFLA) with porcine pancreatic elastase. X-ray studies at…”. X-ray diffraction, 2 ligands (CA, SO4). MolNFT v1 #177752 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7EST
- Type
- protein
- Length
- 241 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P00772
- Ligands
- CA, SO4
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E | — | protein | 241 | — | P00772 |
Ligands and binding sites
- CA · Calcium ion · metal · chains E
- SO4 · Sulfate ion · ion · chains E
- DMF · Dimethylformamide · additive · 5 copies · chains E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7EST · Interaction of the peptide CF3-LEU-ALA-NH-C6H4-CF3(TFLA) with porcine pancreatic… · the same entry in another collection · chain E against E, TM-score 1.00
- P00772 · AlphaFold monomer V2.0 prediction for chymotrypsin-like elastase family member 1 (P00772) · a predicted model of the same protein · chain E 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 P00772
- Elsewhere: RCSB PDB 7EST · PDBe 7EST · UniProt P00772
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