MolNFT v1 · #5685 · protein

A structural comparison of 21 inhibitor complexes of the aspartic proteinase from endothia parasitica

1EPM · Endothiapepsin: “A structural comparison of 21 inhibitor complexes of the aspartic proteinase from endothia parasitica”. X-ray diffraction, 1 ligand (SO4). MolNFT v1 #5685 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 1EPM
Type: protein
Length: 338 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Endothiapepsin; PS2, thr-phe-gln-ala-psa-leu-arg-glu
EC: 3.4.23.22
UniProt: P11838
Ligands: SO4

Structure

x-ray diffraction · 2 distinct chains · 10% helix, 46% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
E	Endothiapepsin (EC 3.4.23.22)	protein	330	11% helix, 46% strand	P11838
I	PS2, thr-phe-gln-ala-psa-leu-arg-glu	protein	8	0% helix, 25% strand	—

Ligands and binding sites

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 · 766 Å² buried · 15 hydrogen bonds · protein-protein

Modifications

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

Compared structures

1EPM · A structural comparison of 21 inhibitor complexes of the aspartic proteinase from… · 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 1EPM · PDBe 1EPM · UniProt P11838

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