Research workbench
Porcine pancreatic elastase complexed with metpheleuglu at pH 5.0
Analyse Porcine pancreatic elastase complexed with metpheleuglu at pH 5.0 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2H1U
- Type
- protein
- Length
- 243 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mfle; Elastase-1
- EC
- 3.4.21.36
- UniProt
- P00772
- Ligands
- CA, SO4
Structure
x-ray diffraction · 2 distinct chains · 11% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| P | Mfle | protein | 3 | 0% helix, 0% strand | — |
| A | Elastase-1 (EC 3.4.21.36) | protein | 240 | 11% helix, 39% strand | P00772 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- P–A · 228 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 2H1U · Porcine pancreatic elastase complexed with MetPheLeuGlu at pH 5.0 · the same entry in another collection · chain P against P, 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 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 P00772
- Elsewhere: RCSB PDB 2H1U · PDBe 2H1U · UniProt P00772
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