Structure of PDB 5lhk Chain A

Receptor sequence
>5lhkA (length=455) Species: 1109705 (Streptomyces sp. BC16019) [Search protein sequence]
AADVVACGRHTGAAVGAFSRRRGFVARPGQVVAEPSADGRAVVLNVGLGP
AGSATAATFRAAAAASVRAVGPARTLRLDLALADGSGVPAAERARAVAEG
AVLGLYRYDEYRSPLAEVIVATPERRAVAEGLAAAEATCLARDLVNCPAG
TLTPPAFADRIRELAHTAGLDCAVYEGAGLTELGLTGLTAVGRGSAEPPR
YVELTYDPPDLTVGLVGKGVTFDSGGLSLKPSGERHAMKADMGGAAAVVA
ALTALPRLGLPLRVRGHLPLAENMPDGGALRVGDVVRHLDGTTTEITHTD
NEGRVVLADVLVRASRPGPHRSDLVVDVATLTSAAVHALGTRTGALFTPD
DRLAQTVLAASERAGESFCRLPLLAHERRNLRSAVADRVNCSHRHGDTIQ
AALFLQDFVAAGVPWAHLDIAAPAYNDEGPYAEVPYGGTGFAVRTLIETL
RALSE
3D structure
PDB5lhk Structure and Substrate Recognition of the Bottromycin Maturation Enzyme BotP.
ChainA
Resolution2.32 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K273 R347
Catalytic site (residue number reindexed from 1) K230 R304
Enzyme Commision number 3.4.11.-
3.4.11.1: leucyl aminopeptidase.
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 MN A K261 D266 D284 E345 K218 D223 D241 E302
BS02 MN A D266 D343 E345 D223 D300 E302
BS03 BCT A N344 G346 R347 L374 N301 G303 R304 L331
Gene Ontology
Molecular Function
GO:0004177 aminopeptidase activity
GO:0008233 peptidase activity
GO:0030145 manganese ion binding
GO:0046872 metal ion binding
GO:0070006 metalloaminopeptidase activity
Biological Process
GO:0006508 proteolysis
GO:0019538 protein metabolic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5lhk, PDBe:5lhk, PDBj:5lhk
PDBsum5lhk
PubMed27653442
UniProtK4MHW2

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