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7ESR

Crystal structure of Synechocystis sp PCC6803 guanidinium hydrolase (R32)

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0008783molecular_functionagmatinase activity
A0016787molecular_functionhydrolase activity
A0016813molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
A0033389biological_processputrescine biosynthetic process from arginine, via agmatine
A0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS01053
Number of Residues22
DetailsARGINASE_1 Arginase family signature. SFDIDcidAgfvPGtgwpepgG
ChainResidueDetails
ASER291-GLY312

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"35264792","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7OI1","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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