Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6WYZ

Crystal structure of Pseudomonas 7A Glutaminase-Asparaginase (mutant K173M) in complex with D-Glu at pH 5.5

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 DGL A 401
ChainResidue
AGLY19
AHOH650
AHOH674
AHOH719
BGLU294
ATHR20
AALA66
ASER67
AGLU68
AGLY99
ATHR100
AASP101
ASER125

site_idAC2
Number of Residues12
Detailsbinding site for residue DGL B 401
ChainResidue
AGLU294
BGLY19
BTHR20
BALA66
BSER67
BGLU68
BGLY99
BTHR100
BASP101
BSER125
BHOH511
BHOH649

site_idAC3
Number of Residues11
Detailsbinding site for residue DGL C 401
ChainResidue
CGLY19
CTHR20
CSER67
CGLU68
CGLY99
CTHR100
CASP101
CSER125
CHOH570
DGLU294
DHOH521

site_idAC4
Number of Residues13
Detailsbinding site for residue DGL D 401
ChainResidue
CGLU294
DGLY19
DTHR20
DALA66
DSER67
DGLU68
DGLY99
DTHR100
DASP101
DSER125
DHOH502
DHOH585
DHOH622

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
DetailsActive site: {"description":"Acyl-ester intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU10099","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10100","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

247035

PDB entries from 2026-01-07

PDB statisticsPDBj update infoContact PDBjnumon