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4AXV

Biochemical and structural characterization of the MpaA amidase as part of a conserved scavenging pathway for peptidoglycan derived peptides in gamma-proteobacteria

Functional Information from GO Data
ChainGOidnamespacecontents
A0004040molecular_functionamidase activity
A0004180molecular_functioncarboxypeptidase activity
A0004181molecular_functionmetallocarboxypeptidase activity
A0005737cellular_componentcytoplasm
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0009253biological_processpeptidoglycan catabolic process
A0016787molecular_functionhydrolase activity
A0016788molecular_functionhydrolase activity, acting on ester bonds
A0016998biological_processcell wall macromolecule catabolic process
A0046872molecular_functionmetal ion binding
A0061473molecular_functionmurein tripeptide carboxypeptidase activity
A0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 301
ChainResidue
AHIS48
AGLU51
AHIS156
AHOH2017

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 302
ChainResidue
AHOH2003
APHE12
ALEU13
AILE14
ALEU62
ALEU65

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01379","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22970852","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4AXV","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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