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6WYY

Crystal structure of Pseudomonas 7A Glutaminase-Asparaginase in complex with L-Glu at pH 6.5

Functional Information from GO Data
ChainGOidnamespacecontents
A0004067molecular_functionasparaginase activity
A0004359molecular_functionglutaminase activity
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
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
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
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 Residues13
Detailsbinding site for residue GLU A 400
ChainResidue
AGLY19
AHOH502
AHOH581
AHOH695
BGLU294
ATHR20
AALA66
ASER67
AGLU68
AGLY99
ATHR100
AASP101
ASER125

site_idAC2
Number of Residues8
Detailsbinding site for residue EDO A 401
ChainResidue
AALA16
ATHR17
AGLY18
AALA22
AGLY40
AGLN61
AGLN64
ATHR97

site_idAC3
Number of Residues7
Detailsbinding site for residue EDO A 402
ChainResidue
ALYS205
ATRP335
AHOH506
AHOH595
AHOH716
DTRP199
DHOH641

site_idAC4
Number of Residues13
Detailsbinding site for residue GLU B 400
ChainResidue
AGLU294
BGLY19
BTHR20
BALA66
BSER67
BGLU68
BGLY99
BTHR100
BASP101
BSER125
BHOH505
BHOH549
BHOH648

site_idAC5
Number of Residues3
Detailsbinding site for residue GOL B 401
ChainResidue
BARG81
BGLU84
BHOH720

site_idAC6
Number of Residues6
Detailsbinding site for residue EDO B 402
ChainResidue
BASN292
BALA293
BGLU294
BGLN295
BPRO296
BHOH615

site_idAC7
Number of Residues13
Detailsbinding site for residue GLU C 400
ChainResidue
CGLY19
CTHR20
CALA66
CSER67
CGLU68
CGLY99
CTHR100
CASP101
CSER125
CHOH608
CHOH645
DGLU294
DHOH516

site_idAC8
Number of Residues7
Detailsbinding site for residue EDO C 401
ChainResidue
CALA32
CTHR33
CTYR34
CHOH550
CHOH725
DALA293
DGLU294

site_idAC9
Number of Residues7
Detailsbinding site for residue EDO C 402
ChainResidue
CASP92
CALA147
CSER148
CASP149
CARG153
CHOH504
CHOH614

site_idAD1
Number of Residues12
Detailsbinding site for residue GLU D 400
ChainResidue
CGLU294
DGLY19
DTHR20
DALA66
DSER67
DGLU68
DGLY99
DTHR100
DASP101
DSER125
DHOH555
DHOH659

site_idAD2
Number of Residues8
Detailsbinding site for residue EDO D 401
ChainResidue
BLYS272
DPRO222
DLYS247
DMET321
DGLN325
DHOH503
DHOH660
DHOH740

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
ATHR20
BTHR20
CTHR20
DTHR20

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

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PDB entries from 2024-10-02

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