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7TDV

Crystal structure of S. aureus glutamine synthetase in Met-Sox-P/ADP transition state complex

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004356molecular_functionglutamine synthetase activity
A0005737cellular_componentcytoplasm
A0006542biological_processobsolete glutamine biosynthetic process
B0003824molecular_functioncatalytic activity
B0004356molecular_functionglutamine synthetase activity
B0005737cellular_componentcytoplasm
B0006542biological_processobsolete glutamine biosynthetic process
C0003824molecular_functioncatalytic activity
C0004356molecular_functionglutamine synthetase activity
C0005737cellular_componentcytoplasm
C0006542biological_processobsolete glutamine biosynthetic process
D0003824molecular_functioncatalytic activity
D0004356molecular_functionglutamine synthetase activity
D0005737cellular_componentcytoplasm
D0006542biological_processobsolete glutamine biosynthetic process
E0003824molecular_functioncatalytic activity
E0004356molecular_functionglutamine synthetase activity
E0005737cellular_componentcytoplasm
E0006542biological_processobsolete glutamine biosynthetic process
H0003824molecular_functioncatalytic activity
H0004356molecular_functionglutamine synthetase activity
H0005737cellular_componentcytoplasm
H0006542biological_processobsolete glutamine biosynthetic process
Functional Information from PROSITE/UniProt
site_idPS00180
Number of Residues19
DetailsGLNA_1 Glutamine synthetase signature 1. FDGSSiegfvrieESDmyL
ChainResidueDetails
APHE54-LEU72

site_idPS00181
Number of Residues16
DetailsGLNA_ATP Glutamine synthetase putative ATP-binding region signature. KPLfgv..NGSGmHfnvS
ChainResidueDetails
ALYS236-SER251

253795

PDB entries from 2026-05-20

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