Structure of PDB 7esr Chain A Binding Site BS01

Receptor Information

>7esr Chain A (length=378) Species: 1148 (Synechocystis sp. PCC 6803)

PPSEAEEALIKETRLPLTGWQQEVDQGLTYGLEAAASIKDRSIPTFSRGE
LPHYAGINTFMKAPYLEDVREVGKYDVAIVGVPHDSGTTYRPGTRFGPQG
IRRISALYTPYNFEMGVDLREQISLCDVGDIFTIPANNEKSFDQISKGIA
HIFSSGAFPIILGGDHSIGFPTVRGICRHLGDKKVGIIHFDRHVDTQETD
LDERMHTCPWFHATNMANAPAKNLVQLGIGGWQVPRQGVKVCRERATNIL
TVTDITEMSLDAAADFAIARATDGTDCVWISFDIDCIDAGFVPGTGWPEP
GGLLPREALYLLKRIIRETNVCGMEVVEVSPPYDISDMTSLMATRVICDT
MAHLVVSGQLPRTEKPAYIHAEANMAVD

Ligand information

• Ligand ID: CA
• InChI: InChI=1S/Ca/q+2
• InChIKey: BHPQYMZQTOCNFJ-UHFFFAOYSA-N
• SMILES:
  CACTVS 3.341: [Ca++]
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Ca+2]
• Formula: Ca
• Name: CALCIUM ION
• DrugBank: DB14577
• PDB chain: 7esr Chain A Residue 501

Receptor-Ligand Complex Structure

Structure summary

• PDB: 7esr Discovery of a Ni 2+ -dependent guanidine hydrolase in bacteria.
• Resolution: 1.42 Å
• Binding residue (original residue number in PDB): D201 H203 D293 D295
• Binding residue (residue number reindexed from 1): D191 H193 D283 D285
• Annotation score: 1

Enzymatic activity

• Enzyme Commision number: 3.5.3.11: agmatinase.

Gene Ontology

Molecular Function

• GO:0008783 agmatinase activity
• GO:0016787 hydrolase activity
• GO:0016813 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
• GO:0046872 metal ion binding

Biological Process

• GO:0033389 putrescine biosynthetic process from arginine, using agmatinase

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:7esr, PDBe:7esr, PDBj:7esr
• PDBsum: 7esr
• PubMed: 35264792
• UniProt: P73270|GDMH_SYNY3 Guanidine hydrolase (Gene Name=gdmH)