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Structure and catalysis of acylaminoacyl peptidase

Analyse Structure and catalysis of acylaminoacyl peptidase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3O4H
Type: protein
Length: 2,302 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q9YBQ2

Structure

x-ray diffraction · 4 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	576	—	Q9YBQ2
B	—	protein	574	—	Q9YBQ2
C	—	protein	577	—	Q9YBQ2
D	—	protein	575	—	Q9YBQ2

Compared structures

3O4H · Structure and Catalysis of Acylaminoacyl Peptidase · the same entry in another collection · chain D against D, TM-score 1.00
Q9YBQ2 · AlphaFold monomer V2.0 prediction for acylamino-acid-releasing enzyme (Q9YBQ2) · a predicted model of the same protein · 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 Q9YBQ2
Elsewhere: RCSB PDB 3O4H · PDBe 3O4H · UniProt Q9YBQ2

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