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3NIQ

Crystal structure of Pseudomonas aeruginosa guanidinopropionase

Functional Information from GO Data
ChainGOidnamespacecontents
A0008783molecular_functionagmatinase 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
A0047972molecular_functionguanidinopropionase activity
B0008783molecular_functionagmatinase activity
B0016813molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
B0033389biological_processputrescine biosynthetic process from arginine, via agmatine
B0046872molecular_functionmetal ion binding
B0047972molecular_functionguanidinopropionase activity
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 1205
ChainResidue
AARG16
APHE17
AASN50
AARG51
AASN63
ASER66
ALEU67
BHIS56
BARG59

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 1601
ChainResidue
AHIS126
AASP148
AASP152
AASP240
AHOH367
AMN1602

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 1602
ChainResidue
AASP148
AHIS150
AASP240
AASP242
AHOH367
AMN1601

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN B 1603
ChainResidue
BHIS126
BASP148
BASP152
BASP240
BHOH371
BMN1604

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN B 1604
ChainResidue
BASP148
BHIS150
BASP240
BASP242
BHOH371
BMN1603

Functional Information from PROSITE/UniProt
site_idPS01053
Number of Residues22
DetailsARGINASE_1 Arginase family signature. SFDVDvldPafaPGtgtpeigG
ChainResidueDetails
ASER238-GLY259

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00742","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21600989","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

251801

PDB entries from 2026-04-08

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