Research workbench
Complex of subtilase subty from bacillus sp. TY145 with chymotrypsin inhibitor CI2A
Analyse Complex of subtilase subty from bacillus sp. TY145 with chymotrypsin inhibitor… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5FFN
- Type
- protein
- Length
- 375 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Enzyme subtilase subty from bacillus sp. TY145; Subtilisin-chymotrypsin inhibitor-2A
- EC
- 3.4.21.14
- UniProt
- P01053
- Ligands
- CA, NA
- Pockets
- 1 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 26% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Enzyme subtilase subty from bacillus sp. TY145 (EC 3.4.21.14) | protein | 311 | 26% helix, 23% strand | — |
| I | Subtilisin-chymotrypsin inhibitor-2A | protein | 64 | 22% helix, 33% strand | P01053 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 153 | 0.72 | 0.91 | 30 | empty |
Interfaces
1 interface between chains.
- A–I · 787 Ų buried · 19 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 5FFN · Complex of subtilase SubTY from Bacillus sp. TY145 with chymotrypsin inhibitor CI2A · the same entry in another collection · chain A against A, TM-score 1.00
- P01053 · AlphaFold monomer V2.0 prediction for subtilisin-chymotrypsin inhibitor-2A (P01053) · a predicted model of the same protein · chain I against A, TM-score 0.95
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 P01053
- Elsewhere: RCSB PDB 5FFN · PDBe 5FFN · UniProt P01053
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