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3CZX

The crystal structure of the putative N-acetylmuramoyl-L-alanine amidase from Neisseria meningitidis

Functional Information from GO Data
ChainGOidnamespacecontents
A0008745molecular_functionN-acetylmuramoyl-L-alanine amidase activity
A0009253biological_processpeptidoglycan catabolic process
A0016787molecular_functionhydrolase activity
A0030288cellular_componentouter membrane-bounded periplasmic space
A0043093biological_processFtsZ-dependent cytokinesis
A0046872molecular_functionmetal ion binding
B0008745molecular_functionN-acetylmuramoyl-L-alanine amidase activity
B0009253biological_processpeptidoglycan catabolic process
B0016787molecular_functionhydrolase activity
B0030288cellular_componentouter membrane-bounded periplasmic space
B0043093biological_processFtsZ-dependent cytokinesis
B0046872molecular_functionmetal ion binding
C0008745molecular_functionN-acetylmuramoyl-L-alanine amidase activity
C0009253biological_processpeptidoglycan catabolic process
C0016787molecular_functionhydrolase activity
C0030288cellular_componentouter membrane-bounded periplasmic space
C0043093biological_processFtsZ-dependent cytokinesis
C0046872molecular_functionmetal ion binding
D0008745molecular_functionN-acetylmuramoyl-L-alanine amidase activity
D0009253biological_processpeptidoglycan catabolic process
D0016787molecular_functionhydrolase activity
D0030288cellular_componentouter membrane-bounded periplasmic space
D0043093biological_processFtsZ-dependent cytokinesis
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN C 301
ChainResidue
CHIS11
CGLU25
CHIS77

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN D 301
ChainResidue
DHIS11
DGLU25
DHIS77

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN A 301
ChainResidue
AHIS11
AGLU25
AHIS77

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN B 301
ChainResidue
BHIS11
BGLU25
BHIS77

247947

PDB entries from 2026-01-21

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