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X-ray studies of aspartic proteinase-statine inhibitor complexes.

Analyse X-ray studies of aspartic proteinase-statine inhibitor complexes. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2ER9
Type: protein
Length: 336 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Endothiapepsin; L363,564
EC: 3.4.23.6
UniProt: P11838
Ligands: BOC

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
E	Endothiapepsin (EC 3.4.23.6)	protein	330	10% helix, 47% strand	P11838
I	L363,564	protein	6	0% helix, 17% strand	—

Ligands and binding sites

BOC · Tert-butyl hydrogen carbonate · ligand · chains E, I

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

Interfaces

1 interface between chains.

E–I · 708 Å² buried · 16 hydrogen bonds · protein-protein

Modifications

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

Compared structures

2ER9 · X-ray studies of aspartic proteinase-statine inhibitor complexes. · 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 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 P11838
Elsewhere: RCSB PDB 2ER9 · PDBe 2ER9 · UniProt P11838

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