Structure of PDB 5lhk Chain A Binding Site BS02

Receptor Information

>5lhk Chain A (length=455) Species: 1109705 (Streptomyces sp. BC16019)

AADVVACGRHTGAAVGAFSRRRGFVARPGQVVAEPSADGRAVVLNVGLGP
AGSATAATFRAAAAASVRAVGPARTLRLDLALADGSGVPAAERARAVAEG
AVLGLYRYDEYRSPLAEVIVATPERRAVAEGLAAAEATCLARDLVNCPAG
TLTPPAFADRIRELAHTAGLDCAVYEGAGLTELGLTGLTAVGRGSAEPPR
YVELTYDPPDLTVGLVGKGVTFDSGGLSLKPSGERHAMKADMGGAAAVVA
ALTALPRLGLPLRVRGHLPLAENMPDGGALRVGDVVRHLDGTTTEITHTD
NEGRVVLADVLVRASRPGPHRSDLVVDVATLTSAAVHALGTRTGALFTPD
DRLAQTVLAASERAGESFCRLPLLAHERRNLRSAVADRVNCSHRHGDTIQ
AALFLQDFVAAGVPWAHLDIAAPAYNDEGPYAEVPYGGTGFAVRTLIETL
RALSE

Ligand information

• Ligand ID: MN
• InChI: InChI=1S/Mn/q+2
• InChIKey: WAEMQWOKJMHJLA-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Mn+2]
  CACTVS 3.341: [Mn++]
• Formula: Mn
• Name: MANGANESE (II) ION
• DrugBank: DB06757
• PDB chain: 5lhk Chain A Residue 602

Receptor-Ligand Complex Structure

Structure summary

• PDB: 5lhk Structure and Substrate Recognition of the Bottromycin Maturation Enzyme BotP.
• Resolution: 2.32 Å
• Binding residue (original residue number in PDB): D266 D343 E345
• Binding residue (residue number reindexed from 1): D223 D300 E302
• Annotation score: 4

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.

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

External links

• PDB: RCSB:5lhk, PDBe:5lhk, PDBj:5lhk
• PDBsum: 5lhk
• PubMed: 27653442
• UniProt: K4MHW2