Research workbench
Crystal structure of proteinase K from engyodontium albuminhibited by methoxysuccinyl-ala-ala-pro-phe-chloromethyl ketone at 1.15 a resolution
Analyse Crystal structure of proteinase K from engyodontium albuminhibited by… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4ZAR
- Type
- protein
- Length
- 283 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Proteinase K; Methoxysuccinyl-ala-ala-pro-phe-chloromethyl ketone, bound form
- EC
- 3.4.21.64
- UniProt
- P06873
- Ligands
- MSU, CA
Structure
x-ray diffraction · 2 distinct chains · 27% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Proteinase K (EC 3.4.21.64) | protein | 279 | 27% helix, 25% strand | P06873 |
| B | Methoxysuccinyl-ala-ala-pro-phe-chloromethyl ketone, bound form | protein | 4 | 0% helix, 50% strand | — |
Ligands and binding sites
- MSU · Succinic acid monomethyl ester · ligand · chains A, B
- CA · Calcium ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 386 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide, 1 covalent, 1 modified (disulfide, covalent ligand, nonstandard).
Compared structures
- 4ZAR · Crystal Structure of Proteinase K from Engyodontium albuminhibited by… · the same entry in another collection · chain A 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 P06873
- Elsewhere: RCSB PDB 4ZAR · PDBe 4ZAR · UniProt P06873
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