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2NV0

Structure of the glutaminase subunit Pdx2 (YaaE) of PLP synthase from Bacillus subtilis

Functional Information from GO Data
ChainGOidnamespacecontents
A0004359molecular_functionglutaminase activity
A0005515molecular_functionprotein binding
A0005829cellular_componentcytosol
A0006541biological_processglutamine metabolic process
A0006543biological_processglutamine catabolic process
A0008614biological_processpyridoxine metabolic process
A0016787molecular_functionhydrolase activity
A0016829molecular_functionlyase activity
A0036381molecular_functionpyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity
A0042802molecular_functionidentical protein binding
A0042819biological_processvitamin B6 biosynthetic process
A0042823biological_processpyridoxal phosphate biosynthetic process
A1903600cellular_componentglutaminase complex
B0004359molecular_functionglutaminase activity
B0005515molecular_functionprotein binding
B0005829cellular_componentcytosol
B0006541biological_processglutamine metabolic process
B0006543biological_processglutamine catabolic process
B0008614biological_processpyridoxine metabolic process
B0016787molecular_functionhydrolase activity
B0016829molecular_functionlyase activity
B0036381molecular_functionpyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity
B0042802molecular_functionidentical protein binding
B0042819biological_processvitamin B6 biosynthetic process
B0042823biological_processpyridoxal phosphate biosynthetic process
B1903600cellular_componentglutaminase complex
Functional Information from PROSITE/UniProt
site_idPS01236
Number of Residues11
DetailsPDXT_SNO_1 PdxT/SNO family family signature. GLILPGGESTT
ChainResidueDetails
AGLY41-THR51

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_01615, ECO:0000305
ChainResidueDetails
ACYS79
BCYS79

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Charge relay system => ECO:0000255|HAMAP-Rule:MF_01615, ECO:0000305
ChainResidueDetails
AHIS170
AGLU172
BHIS170
BGLU172

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01615, ECO:0000269|PubMed:17159152
ChainResidueDetails
AGLY47
AARG106
AILE134
BGLY47
BARG106
BILE134

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1bxr
ChainResidueDetails
AGLU172
AHIS170
ACYS79

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1bxr
ChainResidueDetails
BGLU172
BHIS170
BCYS79

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1bxr
ChainResidueDetails
AHIS170
ACYS79

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1bxr
ChainResidueDetails
BHIS170
BCYS79

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PDB entries from 2024-07-17

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