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7ESR

Crystal structure of Synechocystis sp PCC6803 guanidinium hydrolase (R32)

Functional Information from GO Data
ChainGOidnamespacecontents
A0008783molecular_functionagmatinase activity
A0009446biological_processputrescine biosynthetic process
A0016787molecular_functionhydrolase activity
A0016813molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
A0033389biological_processputrescine biosynthetic process from arginine, using agmatinase
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: BINDING => ECO:0000255|PROSITE-ProRule:PRU00742
ChainResidueDetails
AHIS176
AASP201
AHIS203
AASP205
AASP293
AASP295

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PDB entries from 2024-06-12

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