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6WZ6

Complex of mutant (K173M) of Pseudomonas 7A Glutaminase-Asparaginase with L-Glu at pH 5. Covalent acyl-enzyme intermediate

Functional Information from GO Data
ChainGOidnamespacecontents
A0004067molecular_functionasparaginase activity
A0004359molecular_functionglutaminase activity
A0005829cellular_componentcytosol
A0006520biological_processamino acid metabolic process
A0006528biological_processasparagine metabolic process
A0016787molecular_functionhydrolase activity
A0042597cellular_componentperiplasmic space
A0050417molecular_functionglutamin-(asparagin-)ase activity
B0004067molecular_functionasparaginase activity
B0004359molecular_functionglutaminase activity
B0005829cellular_componentcytosol
B0006520biological_processamino acid metabolic process
B0006528biological_processasparagine metabolic process
B0016787molecular_functionhydrolase activity
B0042597cellular_componentperiplasmic space
B0050417molecular_functionglutamin-(asparagin-)ase activity
C0004067molecular_functionasparaginase activity
C0004359molecular_functionglutaminase activity
C0005829cellular_componentcytosol
C0006520biological_processamino acid metabolic process
C0006528biological_processasparagine metabolic process
C0016787molecular_functionhydrolase activity
C0042597cellular_componentperiplasmic space
C0050417molecular_functionglutamin-(asparagin-)ase activity
D0004067molecular_functionasparaginase activity
D0004359molecular_functionglutaminase activity
D0005829cellular_componentcytosol
D0006520biological_processamino acid metabolic process
D0006528biological_processasparagine metabolic process
D0016787molecular_functionhydrolase activity
D0042597cellular_componentperiplasmic space
D0050417molecular_functionglutamin-(asparagin-)ase activity
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue GLU A 400
ChainResidue
AGLY19
ASER125
AHOH583
AHOH660
BSER258
BGLU294
ATHR20
ATYR34
AALA66
ASER67
AGLU68
AGLY99
ATHR100
AASP101

site_idAC2
Number of Residues8
Detailsbinding site for residue EDO A 401
ChainResidue
ATHR116
AASP117
ALYS118
AGLY154
ALYS155
AGLY156
ATHR208
AHOH623

site_idAC3
Number of Residues10
Detailsbinding site for residue EDO C 401
ChainResidue
CTHR116
CASP117
CGLY154
CLYS155
CGLY156
CHIS207
CTHR208
CVAL209
CHOH517
CHOH588

site_idAC4
Number of Residues3
Detailsbinding site for residue EDO D 401
ChainResidue
DARG206
DGLU212
DARG332

site_idAC5
Number of Residues18
Detailsbinding site for Di-peptide GLU B 400 and THR B 20
ChainResidue
ASER258
AGLU294
BGLY19
BILE21
BALA22
BGLY23
BTYR34
BALA66
BSER67
BGLU68
BGLY99
BTHR100
BASP101
BSER125
BARG127
BPRO128
BHOH612
BHOH642

site_idAC6
Number of Residues18
Detailsbinding site for Di-peptide GLU C 400 and THR C 20
ChainResidue
CGLY19
CILE21
CALA22
CGLY23
CTYR34
CALA66
CSER67
CGLU68
CGLY99
CTHR100
CASP101
CSER125
CARG127
CPRO128
CHOH579
CHOH651
DSER258
DGLU294

site_idAC7
Number of Residues18
Detailsbinding site for Di-peptide GLU D 400 and THR D 20
ChainResidue
CSER258
CGLU294
DGLY19
DILE21
DALA22
DGLY23
DTYR34
DALA66
DSER67
DGLU68
DGLY99
DTHR100
DASP101
DSER125
DARG127
DPRO128
DHOH589
DHOH643

Functional Information from PROSITE/UniProt
site_idPS00144
Number of Residues9
DetailsASN_GLN_ASE_1 Asparaginase / glutaminase active site signature 1. IlATGGTIA
ChainResidueDetails
AILE14-ALA22

site_idPS00917
Number of Residues11
DetailsASN_GLN_ASE_2 Asparaginase / glutaminase active site signature 2. GiVitHGTDTL
ChainResidueDetails
AGLY93-LEU103

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Acyl-ester intermediate => ECO:0000255|PROSITE-ProRule:PRU10099, ECO:0000255|PROSITE-ProRule:PRU10100
ChainResidueDetails
BTHR20
CTHR20
DTHR20
ATHR20

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
CSER67
CTHR100
DSER67
DTHR100
ATHR100
BSER67
BTHR100
ASER67

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PDB entries from 2024-06-12

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