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2YWD

Crystal structure of glutamine amidotransferase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004359molecular_functionglutaminase activity
A0006541biological_processglutamine metabolic process
A0006543biological_processglutamine catabolic process
A0016787molecular_functionhydrolase activity
A0016829molecular_functionlyase activity
A0036381molecular_functionpyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity
A0042819biological_processvitamin B6 biosynthetic process
A0042823biological_processpyridoxal phosphate biosynthetic process
Functional Information from PROSITE/UniProt
site_idPS01236
Number of Residues11
DetailsPDXT_SNO_1 PdxT/SNO family family signature. ALIVPGGESTT
ChainResidueDetails
AALA42-THR52

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_01615
ChainResidueDetails
ACYS81

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Charge relay system => ECO:0000255|HAMAP-Rule:MF_01615
ChainResidueDetails
AHIS172
AGLU174

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01615
ChainResidueDetails
AGLY48
AARG109
AILE136

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1bxr
ChainResidueDetails
ACYS81
AHIS172
AGLU174

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1bxr
ChainResidueDetails
ACYS81
AHIS172

223532

PDB entries from 2024-08-07

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