Research workbench
Crystal structure of human uropepsin at 2.45 a resolution
Analyse Crystal structure of human uropepsin at 2.45 a resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1FLH
- Type
- protein
- Length
- 326 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uropepsin
- EC
- 3.4.23.1
- UniProt
- P00790
- Pockets
- 2 · best druggability 0.60
Structure
x-ray diffraction · 1 distinct chain · 16% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uropepsin (EC 3.4.23.1) | protein | 326 | 16% helix, 45% strand | P00790 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 325 | 0.60 | 0.77 | 38 | empty |
| 2 | 59 | 0.28 | 0.74 | 18 | empty |
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 1FLH · Crystal structure of human uropepsin at 2.45 a resolution · the same entry in another collection · 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 P00790
- Elsewhere: RCSB PDB 1FLH · PDBe 1FLH · UniProt P00790
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