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The active site of aspartic proteinases

Analyse The active site of aspartic proteinases in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4ER2
Type: protein
Length: 335 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Endothiapepsin; Pepstatin
EC: 3.4.23.6
UniProt: P11838
Ligands: IVA, SO4

Structure

x-ray diffraction · 2 distinct chains · 10% helix, 45% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
E	Endothiapepsin (EC 3.4.23.6)	protein	330	10% helix, 45% strand	P11838
I	Pepstatin	protein	5	0% helix, 0% strand	—

Ligands and binding sites

IVA · Isovaleric acid · ligand · chains E, I
SO4 · Sulfate ion · ion · 3 copies · chains E

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Interfaces

1 interface between chains.

E–I · 575 Å² buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified, 1 covalent, 1 disulfide (nonstandard, covalent ligand, disulfide).

Compared structures

4ER2 · The active site of aspartic proteinases · the same entry in another collection · chain E against E, TM-score 1.00
P11838 · AlphaFold monomer V2.0 prediction for endothiapepsin (P11838) · a predicted model of the same protein · chain E against A, TM-score 0.99

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 P11838
Elsewhere: RCSB PDB 4ER2 · PDBe 4ER2 · UniProt P11838

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