Structure of PDB 6a9u Chain A Binding Site BS03

Receptor Information
>6a9u Chain A (length=405) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GELTPGISALEYYERRIRLAETLPPKSCVILAGNDIQYPFQQENDLFYLS
GWNEPNSVMILEKPTDSLSDTIFHMLVPPFRSGVYGVQEIFNADESASIN
DLSKYLPKIINRNEFIYFDMLSSSNFKHIKSLLDNKTIKPISKRIAEFRK
IKSPQELRIMRRAGQISGRSFNQAFAKRFRNERTLDSFLHYKFISGGCDK
DAYIPVVATGSNSLCIHYTRNDDVMFDDEMVLVDAAGSLGGYCADISRTW
PNSGKFTDAQRDLYEAVLNVQRDCIKLCKASNNYSLHDIHEKSITLMKQE
LKNLGIDKVSGWNVEKLYPHYIGHNLGLDVHDVPKVSRYEPLKVGQVITI
EPGLYIPNEESFPSYFRNVGIRIEDDIAIGEDTYTNLTVEAVKEIDDLEN
VMQNG
Ligand information
Ligand IDMN
InChIInChI=1S/Mn/q+2
InChIKeyWAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mn+2]
CACTVS 3.341[Mn++]
FormulaMn
NameMANGANESE (II) ION
ChEMBL
DrugBankDB06757
ZINC
PDB chain6a9u Chain A Residue 602 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB6a9u Crystal structures and biochemical analyses of intermediate cleavage peptidase: role of dynamics in enzymatic function.
Resolution2.4 Å
Binding residue
(original residue number in PDB)
D338 H417 E444 E467
Binding residue
(residue number reindexed from 1)
D245 H324 E351 E374
Annotation score4
Enzymatic activity
Enzyme Commision number 3.4.11.26: intermediate cleaving peptidase 55.
Gene Ontology
Molecular Function
GO:0030145 manganese ion binding
GO:0070006 metalloaminopeptidase activity

View graph for
Molecular Function
External links
PDB RCSB:6a9u, PDBe:6a9u, PDBj:6a9u
PDBsum6a9u
PubMed30582634
UniProtP40051|ICP55_YEAST Intermediate cleaving peptidase 55 (Gene Name=ICP55)

[Back to BioLiP]