Research workbench
Prosubtilisin substrate complex of subtilisin SUBT_BACAM
Analyse Prosubtilisin substrate complex of 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
- 3CNQ
- Type
- protein
- Length
- 335 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
Structure
x-ray diffraction · 2 distinct chains · 30% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| P | Subtilisin bpn' | protein | 71 | 24% helix, 37% strand | P00782 |
| S | Subtilisin bpn' (EC 3.4.21.62) | protein | 264 | 31% helix, 21% strand | P00782 |
Ligands and binding sites
- ZN · Zinc ion · metal · 5 copies · chains S
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- P–S · 1180 Ų buried · 30 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 3CNQ · Prosubtilisin Substrate Complex of 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 3CNQ · PDBe 3CNQ · UniProt P00782
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