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1ZQ1

Structure of GatDE tRNA-Dependent Amidotransferase from Pyrococcus abyssi

Functional Information from GO Data
ChainGOidnamespacecontents
A0004067molecular_functionasparaginase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0006412biological_processtranslation
A0006450biological_processregulation of translational fidelity
A0006520biological_processamino acid metabolic process
A0016874molecular_functionligase activity
A0050567molecular_functionglutaminyl-tRNA synthase (glutamine-hydrolyzing) activity
B0004067molecular_functionasparaginase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0006412biological_processtranslation
B0006450biological_processregulation of translational fidelity
B0006520biological_processamino acid metabolic process
B0016874molecular_functionligase activity
B0050567molecular_functionglutaminyl-tRNA synthase (glutamine-hydrolyzing) activity
C0003824molecular_functioncatalytic activity
C0004812molecular_functionaminoacyl-tRNA ligase activity
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0006412biological_processtranslation
C0016874molecular_functionligase activity
C0016884molecular_functioncarbon-nitrogen ligase activity, with glutamine as amido-N-donor
C0050567molecular_functionglutaminyl-tRNA synthase (glutamine-hydrolyzing) activity
D0003824molecular_functioncatalytic activity
D0004812molecular_functionaminoacyl-tRNA ligase activity
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0006412biological_processtranslation
D0016874molecular_functionligase activity
D0016884molecular_functioncarbon-nitrogen ligase activity, with glutamine as amido-N-donor
D0050567molecular_functionglutaminyl-tRNA synthase (glutamine-hydrolyzing) activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ASP A 1000
ChainResidue
APHE145
ASER146
AGLU147
ATHR178
AASP179
AALA204
BTYR376

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ASP B 5000
ChainResidue
BGLU147
BTHR178
BASP179
BGLN205
ATYR376
BSER146

Functional Information from PROSITE/UniProt
site_idPS00144
Number of Residues9
DetailsASN_GLN_ASE_1 Asparaginase / glutaminase active site signature 1. IiGTGGTIA
ChainResidueDetails
AILE96-ALA104

site_idPS00917
Number of Residues11
DetailsASN_GLN_ASE_2 Asparaginase / glutaminase active site signature 2. GvVvaHGTDTM
ChainResidueDetails
AGLY171-MSE181

site_idPS01234
Number of Residues15
DetailsGATB Glutamyl-tRNA(Gln) amidotransferase subunit B signature. LDRlgiPLIEIsTtP
ChainResidueDetails
CLEU180-PRO194

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00586
ChainResidueDetails
ATHR102
ATHR178
AASP179
ALYS256
BTHR102
BTHR178
BASP179
BLYS256

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 3eca
ChainResidueDetails
ATHR102
AASP179
ATHR178
ATYR115
ALYS256

site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 3eca
ChainResidueDetails
BTHR102
BASP179
BTHR178
BTYR115
BLYS256

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 3eca
ChainResidueDetails
ATHR102
ATHR178
ATYR115
BSER377

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 3eca
ChainResidueDetails
ASER377
BTHR102
BTYR115
BTHR178

site_idCSA5
Number of Residues1
DetailsAnnotated By Reference To The Literature 3eca
ChainResidueDetails
AGLY379

site_idCSA6
Number of Residues1
DetailsAnnotated By Reference To The Literature 3eca
ChainResidueDetails
BGLY379

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PDB entries from 2024-07-24

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