Structure of PDB 6zeq Chain A

Receptor sequence
>6zeqA (length=301) Species: 510516 (Aspergillus oryzae RIB40) [Search protein sequence]
AVTYPDSVQHNETVQNLIKSLDKKNFETVLQPFSEFHNRYYKSDNGKKSS
EWLQGKIQEIISASGAKGVTVEPFKHSFPQSSLIAKIPGKSDKTIVLGAH
QDSINLDSPSEGRAPGADDDGSGVVTILEAFRVLLTDEKVAAGEAPNTVE
FHFYAGEEGGLLGSQDIFEQYSQKSRDVKAMLQQDMTGYTKGTTDAGKPE
SIGIITDNVDENLTKFLKVIVDAYCTIPTVDSKCGYGCSDHASATKYGYP
AAFAFESAFGDDSPYIHSADDTIETVNFDHVLQHGRLTLGFAYELAFADS
L
3D structure
PDB6zeq The role of propeptide-mediated autoinhibition and intermolecular chaperone in the maturation of cognate catalytic domain in leucine aminopeptidase.
ChainA
Resolution1.97 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) H176 D195 E233 E234 D261 H343
Catalytic site (residue number reindexed from 1) H100 D119 E157 E158 D185 H267
Enzyme Commision number 3.4.11.-
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 ZN A H176 D195 D261 H100 D119 D185
BS02 ZN A D195 E234 H343 D119 E158 H267
Gene Ontology
Molecular Function
GO:0008235 metalloexopeptidase activity
Biological Process
GO:0006508 proteolysis

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:6zeq, PDBe:6zeq, PDBj:6zeq
PDBsum6zeq
PubMed33989771
UniProtQ2U1F3|LAPA_ASPOR Leucine aminopeptidase A (Gene Name=lapA)

[Back to BioLiP]