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3NG0

Crystal Structure of Glutamine Synthetase from Synechocystis sp. PCC 6803

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004356molecular_functionglutamine synthetase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006542biological_processglutamine biosynthetic process
A0016020cellular_componentmembrane
A0016874molecular_functionligase activity
A0019676biological_processammonia assimilation cycle
A0019740biological_processnitrogen utilization
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE ANP A 474
ChainResidue
ATYR128
AARG342
AARG347
ALYS356
AARG359
AGLU361
AMN475
AMN476
AMN477
AGLU132
AGLU210
ALYS211
AILE226
ALYS227
APHE228
AHIS274
ASER276

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MN A 475
ChainResidue
AGLU134
AGLU215
AGLU223
AANP474

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MN A 476
ChainResidue
AGLU132
AANP474

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN A 477
ChainResidue
AGLU132
AHIS272
AGLU361
AARG363
AANP474

Functional Information from PROSITE/UniProt
site_idPS00180
Number of Residues19
DetailsGLNA_1 Glutamine synthetase signature 1. FDGSSirgwkainESDmcM
ChainResidueDetails
APHE52-MET70

site_idPS00181
Number of Residues16
DetailsGLNA_ATP Glutamine synthetase putative ATP-binding region signature. KPIfnd..NGSGmHvhqS
ChainResidueDetails
ALYS261-SER276

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING: BINDING => ECO:0000305|Ref.6, ECO:0007744|PDB:3NG0
ChainResidueDetails
AGLU132
AGLU210
ASER276
AARG347
ALYS356

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|Ref.6, ECO:0007744|PDB:3NG0
ChainResidueDetails
AGLU134
AGLU215
AGLU223
AGLU361

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P9WN39
ChainResidueDetails
AASN267
AHIS272
AHIS274
AARG342

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P12425
ChainResidueDetails
AGLY268

site_idSWS_FT_FI5
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P0A1P6
ChainResidueDetails
AARG324
AGLU330
AARG363

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: O-AMP-tyrosine => ECO:0000250|UniProtKB:P9WN39
ChainResidueDetails
ATYR401

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PDB entries from 2024-07-24

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