Research workbench
Three-dimensional structure of the alkaline protease of pseudomonas aeruginosa: a two-domain protein with a calcium binding parallel beta roll motif
Analyse Three-dimensional structure of the alkaline protease of pseudomonas aeruginosa… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1KAP
- Type
- protein
- Length
- 474 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alkaline protease; Tetrapeptide (gly ser asn ser)
- EC
- 3.4.24.-
- UniProt
- Q03023
- Ligands
- CA, ZN
- Pockets
- 2 · best druggability 0.40
Structure
x-ray diffraction · 2 distinct chains · 18% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| P | Alkaline protease (EC 3.4.24.-) | protein | 470 | 18% helix, 23% strand | Q03023 |
| I | Tetrapeptide (gly ser asn ser) | protein | 4 | 0% helix, 25% strand | — |
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 | 80 | 0.40 | 0.79 | 16 | empty |
| 2 | 89 | 0.36 | 0.75 | 18 | empty |
Interfaces
1 interface between chains.
- P–I · 384 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 1KAP · Three-dimensional structure of the alkaline protease of pseudomonas aeruginosa: a… · the same entry in another collection · chain P against P, TM-score 1.00
- Q03023 · AlphaFold monomer V2.0 prediction for serralysin (Q03023) · a predicted model of the same protein · chain P 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 Q03023
- Elsewhere: RCSB PDB 1KAP · PDBe 1KAP · UniProt Q03023
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