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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: 1ER8
Type: protein
Length: 338 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Endothiapepsin; H-77
EC: 3.4.23.22
UniProt: P11838

Structure

x-ray diffraction · 2 distinct chains · 11% helix, 45% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
E	Endothiapepsin (EC 3.4.23.22)	protein	330	11% helix, 46% strand	P11838
I	H-77	protein	8	0% helix, 13% strand	—

Interfaces

1 interface between chains.

E–I · 774 Å² buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 d-amino, 1 disulfide (D-amino acid, disulfide).

Compared structures

1ER8 · 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 1ER8 · PDBe 1ER8 · UniProt P11838

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