MolNFT v1 · #118888 · protein
Complex of subtilase subty from bacillus sp. TY145 with chymotrypsin inhibitor CI2A
5FFN · Enzyme subtilase subty from bacillus sp. TY145: “Complex of subtilase subty from bacillus sp. TY145 with chymotrypsin inhibitor CI2A”. X-ray diffraction, 2 ligands (CA, NA), 1 pocket (best druggability 0.72). MolNFT v1 #118888 on…
- 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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