Research workbench
High resolution crystal structure of mutant E23A of kumamolisin, a sedolisin type proteinase (previously called kumamolysin or kscp)
Analyse High resolution crystal structure of mutant E23A of kumamolisin, a sedolisin… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1T1G
- Type
- protein
- Length
- 357 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Kumamolisin
- UniProt
- Q8RR56
- Ligands
- CA, SO4
- Pockets
- 2 · best druggability 0.34
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Kumamolisin | protein | 357 | 30% helix, 22% strand | Q8RR56 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 99 | 0.34 | 0.74 | 27 | empty |
| 2 | 63 | 0.31 | 0.75 | 15 | empty |
Compared structures
- 1T1G · High Resolution Crystal Structure of Mutant E23A of Kumamolisin, a sedolisin type… · 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 Q8RR56
- Elsewhere: RCSB PDB 1T1G · PDBe 1T1G · UniProt Q8RR56
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