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8PVG

Structure of E. coli glutamine synthetase determined by cryoEM at 100 keV

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004356molecular_functionglutamine synthetase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006542biological_processglutamine biosynthetic process
A0009314biological_processresponse to radiation
A0016020cellular_componentmembrane
A0016874molecular_functionligase activity
A0016879molecular_functionligase activity, forming carbon-nitrogen bonds
A0019676biological_processammonia assimilation cycle
A0019740biological_processnitrogen utilization
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS00180
Number of Residues19
DetailsGLNA_1 Glutamine synthetase signature 1. FDGSSiggwkginESDmvL
ChainResidueDetails
APHE50-LEU68

site_idPS00181
Number of Residues16
DetailsGLNA_ATP Glutamine synthetase putative ATP-binding region signature. KPMfgd..NGSGmHchmS
ChainResidueDetails
ALYS259-SER274

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P9WN39
ChainResidueDetails
AGLU130
AGLU132
AGLU213
AGLU221
AHIS270
AARG340
AARG345
AGLU358

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P0A1P6
ChainResidueDetails
AGLU208
AASN265
AHIS272
AARG322
AGLU328
AARG360

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P12425
ChainResidueDetails
AGLY266

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P77961
ChainResidueDetails
ASER274
ALYS353

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: O-AMP-tyrosine => ECO:0000269|PubMed:4904088, ECO:0000269|PubMed:5543675
ChainResidueDetails
APHE398

222415

PDB entries from 2024-07-10

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