Research workbench
Azide complex of engineered subtilisin SUBT_BACAM
Analyse Azide complex of engineered subtilisin SUBT_BACAM in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3BGO
- Type
- protein
- Length
- 334 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Subtilisin bpn'
- EC
- 3.4.21.62
- UniProt
- P00782
- Ligands
- ZN, AZI
Structure
x-ray diffraction · 2 distinct chains · 31% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| P | Subtilisin bpn' | protein | 71 | 25% helix, 37% strand | P00782 |
| S | Subtilisin bpn' (EC 3.4.21.62) | protein | 263 | 32% helix, 22% strand | P00782 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- P–S · 1259 Ų buried · 31 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 3BGO · Azide complex of Engineered Subtilisin SUBT_BACAM · the same entry in another collection · chain P against P, 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 P00782
- Elsewhere: RCSB PDB 3BGO · PDBe 3BGO · UniProt P00782
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